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Record 1 from
database: MEDLINE
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- Title
- Acute aluminium intoxication: a study of the
efficacy of several antidotal treatments in
mice.
- Author
- Domingo JL; Llobet JM; Gómez M; Corbella J
- Address
- Source
- Res Commun Chem Pathol Pharmacol, 1986 Jul,
53:1, 93-104
- Abstract
- The effect of the chelating agents
deferoxamine mesylate (DFOA), sodium salicylate,
citric acid, Na2Ca-ethylendiaminetetracetate
(EDTA), nitrilotriacetic acid (NTA), L-cysteine,
N-acetyl-L-cysteine (NAC) and 2,
3-dimercaptosuccinic acid (DMSA) on the
lethality, elimination and tissue retention of
aluminum was investigated on male Swiss mice. To
determine the effect of the various chelators on
the lethality of aluminium, various doses of Al
(NO3)3.9H2O (3.0 - 7.5 mmol/kg) were given
intraperitoneally followed immediately by the ip
administration of the chelator (at dose equal to
one-third of their respective LD50). Survival
was recorded at the end of 14 days. Significant
increases in survival were noted with citric
acid and DFOA. A decrease of the aluminium
concentration in various tissues, and an
increase in urinary and fecal elimination of
aluminium were also noted with citric acid, DFOA,
and sodium salicylate. Citric acid appear to be
the most effective agent of those tested in the
prevention of acute aluminum intoxication.
- Language of Publication
- English
- Unique Identifier
- 86315107
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- MeSH Heading (Major)
- Aluminum|ME/*TO; Chelating Agents|*PD
- MeSH Heading
- Animal; Citrates|PD; Cysteine|PD;
Deferoxamine|PD; Lethal Dose 50; Male; Mice;
Sodium Salicylate|PD; Tissue Distribution
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0034-5164
- Country of Publication
- UNITED STATES
Record 2 from
database: MEDLINE
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- Title
- Isolation and characterization of wheat
aluminum-regulated genes: possible involvement
of aluminum as a pathogenesis response elicitor.
- Author
- Hamel F; Breton C; Houde M
- Address
- DÆepartement des Sciences biologiques,
UniversitÆe du QuÆebec Äa MontrÆeal, Canada.
- Source
- Planta, 1998 Aug, 205:4, 531-8
- Abstract
- Using differential screening of a root tip
cDNA library prepared from an Al-tolerant wheat
cultivar (Triticum aestivum L. cv. Atlas-66)
exposed to Al, we have isolated and
characterized several wheat aluminum-regulated
(War) cDNAs. Sequence comparison revealed that
genes up-regulated by Al correspond to
peroxidase (war4.2), cysteine proteinase
(war5.2), phenylalanine-ammonia lyase (war7.2),
and oxalate oxidase (war13.2). Two wheat
cultivars that differ in their level of
tolerance (cv. Atlas-66: tolerant, and cv.
Fredrick: sensitive) were used to evaluate the
relationship between the accumulation of War
mRNAs and Al toxicity, as measured by root
growth inhibition (RGI). The mRNA accumulation
was modulated to similar levels in both
cultivars compared at equivalent RGIs. This
indicates that War mRNA accumulation is
associated with the toxicity of Al rather than
with the cultivar's tolerance. It appears that
most of the genes found to be up-regulated by Al
share homologies with genes induced by
pathogens. This suggests that Al may act as an
elicitor of a pathogenesis-related transduction
pathway. The potential functions of the
up-regulated war genes in cell wall
strengthening and Al trapping are discussed.
- Language of Publication
- English
- Unique Identifier
- 98348982
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- MeSH Heading (Major)
- Aluminum|*ME/PD; Cysteine Endopeptidases|*GE/ME;
Genes, Plant|*; Oxidoreductases|*GE/ME; Plant
Proteins|*GE; Wheat|*EN/GE
- MeSH Heading
- Amino Acid Sequence; Base Sequence; DNA,
Plant; Gene Expression Regulation, Plant;
Molecular Sequence Data; Plant Roots|GD;
Sequence Analysis, DNA; Sequence Homology, Amino
Acid; Support, Non-U.S. Gov't; Up-Regulation
(Physiology)
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0032-0935
- Country of Publication
- GERMANY
Record 3 from
database: MEDLINE
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- Title
- The influence of various adjuvants on antibody
synthesis following immunization with an hapten.
- Author
- Kellner J; Erhard M; Schranner I; Lösch U
- Address
- Institut fÂur Physiologie, Physiologische
Chemie und ErnÂahrungsphysiologie,
TierÂarztliche FakultÂat, Ludwig-Maximilians-UniversitÂat
MÂunchen, Germany.
- Source
- Biol Chem Hoppe Seyler, 1992 Jan, 373:1, 51-5
- Abstract
- For the production of specific antibodies to
the hapten MATP
(4-Amino-1,2,2-trimethyl-phenylphosphonate) in
Balb/c mice various non-toxic adjuvants were
compared to Freund's complete adjuvant (FCA).
For immunization the hapten MATP was coupled to
the carrier human serum albumin (HSA). The
immunostimulating effect of the synthetic
lipopeptides Pam3Cys-OH, Pam3Cys-Ser-Ser-Asn-Ala
and different concentrations of the
lipohexapeptide Pam3Cys-Ser-(Lys)4 (Pam3Cys =
S-[2,3-bis(palmitoyloxy)-(2RS)-propyl]-N-
palmitoyl-(R)-cysteine as well as of aluminium
hydroxide were tested. IgG antibody titers in
serum were determined in ELISA. In dose-response
studies 50 micrograms Pam3Cys-Ser-(Lys)4 per
mouse was the most effective dose with a long
period of high antibody levels after the second
booster. Pam3Cys-Ser-Ser-Asn-Ala provoked only
low antibody titers. Immunostimulation with
Pam3Cys--OH did not result in an increased
production of specific antibodies. Compared to
the control group an enhanced antibody synthesis
could be provoked with aluminium hydroxide.
However, the increase was much smaller than by
using FCA. The lipopeptide Pam3Cys-Ser-(Lys)4
turned out to be a very potent adjuvant. One
week after booster injection into mice 50
micrograms of this substance helped to elicit a
higher antibody titer than FCA. Hence, as far as
the degree of antibody production is concerned,
Pam3Cys-Ser--(Lys)4 represents an alternative
adjuvant to FCA.
- Language of Publication
- English
- Unique Identifier
- 92162200
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- MeSH Heading (Major)
- Adjuvants, Immunologic|*PD; Antibody
Formation|*DE
- MeSH Heading
- Aluminum Hydroxide|PD; Amino Acid Sequence;
Animal; Cysteine|AA/PD; Freund's Adjuvant|PD;
Haptens|IM; Immunization; Lipoproteins|PD; Mice;
Mice, Inbred BALB C; Molecular Sequence Data;
Oligopeptides|PD
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0177-3593
- Country of Publication
- GERMANY
Record 4 from
database: MEDLINE
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- Title
- The inhibition of metabolic oxalate production
by sulfhydryl compounds.
- Author
- Bais R; Rofe AM; Conyers RA
- Address
- Division of Clinical Chemistry, Institute of
Medical and Veterinary Science, Adelaide,
Australia.
- Source
- J Urol, 1991 Jun, 145:6, 1302-5
- Abstract
- A number of sulfhydryl compounds were shown to
inhibit CO2 and oxalate formation from
glyoxylate by rat liver homogenates and
hepatocytes. The most significant inhibition
occurred with cysteine and this inhibition was
concentration-dependent. In rats made
hyperoxaluric by administering ethylene glycol
in their drinking water, daily intraperitoneal
injections of cysteine caused a rapid and marked
decrease in urinary oxalate excretion which was
maintained over the duration of the treatment
(28 days). Over this time period, the level of
urinary oxalate excretion in these ethylene
glycol-treated rats was reduced to that of the
controls. It is postulated that the decrease is
due to the formation of a cysteine-glyoxylate
adduct, 2-carboxy-4-thiazolidine carboxylate,
which prevents glyoxylate being further oxidized
to oxalate. Cysteine or similar sulphydryl
compounds may therefore have potential as
therapeutic agents in the prevention of renal
stones.
- Language of Publication
- English
- Unique Identifier
- 91237921
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- MeSH Heading (Major)
- Aluminum|*AI; Liver|*DE; Oxalates|*ME/UR;
Sulfhydryl Compounds|*PD
- MeSH Heading
- Animal; Carbon Dioxide|ME; Cysteine|PD;
Ethylene Glycols; Hyperoxaluria|CI/DT/UR; In
Vitro; Rats; Support, Non-U.S. Gov't
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0022-5347
- Country of Publication
- UNITED STATES
Record 5 from
database: MEDLINE
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- Title
- Factor X-activating procoagulant in normal and
malignant breast tissue.
- Author
- el Baruni K; Taylor I; Roath S; Francis JL
- Address
- University Department of Haematology,
Southampton General Hospital, U.K.
- Source
- Hematol Oncol, 1990 Nov, 8:6, 323-32
- Abstract
- Factor X-activating activity (FXAA) was
determined by a chromogenic assay in normal and
malignant breast tissue. FXAA was found in all
tissue (n = 38) irrespective of pathology, and
the activity of normal tissue was similar to
that of tumours. FXAA correlated with tissue
hemoglobin in normal breast (p less than 0.02)
but not in tumours. FXAA was markedly reduced by
aluminium hydroxide, barium citrate, anti-human
factor VII, DFP, PMSF and phospholipase C, but
was unaffected by iodoacetamide and mercuric
chloride. It is concluded that FXAA is a serine
protease with the properties of a tissue
factor-factor VII complex. FXAA occurs in normal
and malignant breast tissue, although the
'normal' activity may be an artefact of the
homogenization process.
- Language of Publication
- English
- Unique Identifier
- 91139080
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- MeSH Heading (Major)
- Breast|*CH; Breast Neoplasms|*CH; Cysteine
Endopeptidases|*AN/ME
- MeSH Heading
- Adsorption; Aluminum Hydroxide|PD; Citrates|PD;
Factor VII|PD; Female; Hemoglobins|AN; Human;
Isoflurophate|PD; Neoplasm Proteins|AN;
Phenylmethylsulfonyl Fluoride|PD; Phospholipase
C|PD
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0278-0232
- Country of Publication
- ENGLAND
Record 6 from
database: MEDLINE
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- Title
- Conformational changes at the carboxyl
terminus of Galpha occur during G protein
activation.
- Author
- Yang CS; Skiba NP; Mazzoni MR; Hamm HE
- Address
- Department of Physiology & Biophysics,
College of Medicine, University of Illinois at
Chicago, Chicago, Illinois 60612, USA.
- Source
- J Biol Chem, 1999 Jan, 274:4, 2379-85
- Abstract
- To understand the dynamics of conformational
changes during G protein activation, surface
exposed cysteine residues on Galpha were
fluorescently labeled. Limited trypsinolysis and
mutational analysis of recombinant Galphat/Galphai1
determined that two cysteines are the major
fluorescent labeling sites, Cys210, located in
the switch II region, and Cys347 at the C
terminus. Mutants with serines replacing Cys210
(Chi6a) and Cys347 (Chi6b) were single
fluorescently labeled with lucifer yellow (LY),
while a double mutant (Chi6ab) was no longer
labeled. When Chi6b was labeled with LY on
Cys210, AlF4- caused a 220% increase in LY
fluorescence, indicating that the fluorescent
group at Cys210 is a reporter of conformational
change in the switch II region. Chi6a labeled at
Cys347 also showed an AlF4--dependent increase
in LY fluorescence (91%), indicating that Galpha
activation leads to a conformational change at
the COOH terminus. Preactivation of the protein
with AlF4- before labeling led to a decreased
incorporation of LY into Cys347 suggesting that
Galpha activation buries Cys347. This COOH-terminal
conformational change may provide the structural
basis for communication between the GDP-binding
site on Galpha and activated receptors, and may
contribute to dissociation of activated Galpha
subunit from activated receptor.
- Language of Publication
- English
- Unique Identifier
- 99107896
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- MeSH Heading (Major)
- GTP-Binding Proteins|CH/*ME
- MeSH Heading
- Aluminum Compounds|CH; Chimeric Proteins|CH/ME;
Chromatography, High Pressure Liquid;
Cysteine|CH; Fluorescent Dyes|CH; Fluorides|CH;
Isoquinolines|CH; Protein Conformation;
Solvents; Support, U.S. Gov't, P.H.S.
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0021-9258
- Country of Publication
- UNITED STATES
Record 7 from
database: MEDLINE
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- Title
- Importance of F1-ATPase residue alpha-Arg-376
for catalytic transition state stabilization.
- Author
- Nadanaciva S; Weber J; Wilke Mounts S; Senior
AE
- Address
- Department of Biochemistry and Biophysics,
University of Rochester Medical Center, New York
14642, USA.
- Source
- Biochemistry, 1999 Nov, 38:47, 15493-9
- Abstract
- The functional role of essential residue
alpha-Arg-376 in the catalytic site of F1-ATPase
was studied. The mutants alpha R376C, alpha
R376Q, and alpha R376K were constructed, and
combined with the mutation beta Y331W, to
investigate catalytic site nucleotide-binding
parameters, and to assess catalytic transition
state formation by measurement of
MgADP-fluoroaluminate binding. Each mutation
caused large impairment of ATP synthesis and
hydrolysis. Despite the apparent proximity of
alpha-Arg-376 to bound nucleoside di- and
triphosphate in published X-ray structures, the
mutations had little effect on MgADP or MgATP
binding affinities, particularly at the highest
affinity catalytic site, site 1. Both Cys and
Gln mutants abolished transition state
formation, demonstrating that alpha-Arg-376 is
normally involved at this step of catalysis. A
model of the F1-ATPase catalytic transition
state structure is presented and discussed. The
Lys mutant, although severely impaired,
supported transition state formation, suggesting
that an additional essential role for the
alpha-Arg-376 guanidinium group exists, likely
in alpha/beta conformational signal transmission
required for steady-state catalysis. Parallels
between alpha-Arg-376 and GAP/G-protein "arginine
finger" residues are evident.
- Language of Publication
- English
- Unique Identifier
- 20039872
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- MeSH Heading (Major)
- Arginine|*CH/GE/ME; H(+)-Transporting ATP
Synthase|*CH/GE/ME
- MeSH Heading
- Adenosine Diphosphate|ME; Adenosine
Triphosphate|ME; Aluminum|ME; Binding Sites|GE;
Catalysis; Cysteine|GE; Enzyme Stability|GE;
Escherichia coli|EN/GE; Fluorine|ME;
Glutamine|GE; Lysine|GE; Models, Molecular;
Mutagenesis, Site-Directed; Spectrometry,
Fluorescence; Support, U.S. Gov't, P.H.S.;
Tryptophan|GE; Tyrosine|GE
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0006-2960
- Country of Publication
- UNITED STATES
Record 8 from
database: MEDLINE
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- Title
- Sulphydryl-containing agents: a new approach
to the problem of refractory peptic ulceration.
- Author
- Salim AS
- Address
- University Department of Surgery, Medical
City, Baghdad, Iraq.
- Source
- Pharmacology, 1992, 45:6, 301-6
- Abstract
- Refractory peptic ulceration is the term
applied to those gastric and duodenal ulcers
which remain unhealed despite active treatment
for at least 3 months. Sulphydryl-containing
agents stimulate the formation of
gastrointestinal mucus, bind the oxygen-derived
free radicals that mediate tissue damage and
play an important role in protein synthesis.
This is the first report which suggests that
these agents stimulate the healing of refractory
gastric and duodenal ulceration without any
adverse events.
- Language of Publication
- English
- Unique Identifier
- 93141659
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- MeSH Heading (Major)
- Anti-Ulcer Agents|*TU; Peptic Ulcer|*DT;
Sulfhydryl Compounds|*TU
- MeSH Heading
- Adult; Aluminum Hydroxide|TU; Antacids|TU;
Cimetidine|TU; Cysteine|TU; Drug Combinations;
Drug Therapy, Combination; Endoscopy,
Gastrointestinal; Female; Human; Magnesium
Hydroxide|TU; Male; Middle Age; Vitamin U|TU
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0031-7012
- Country of Publication
- SWITZERLAND
Record 9 from
database: MEDLINE
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- Title
- High performance liquid chromatographic
separation of cisplatin and its hydrolysis
products on alumina and application to studies
of their interaction with cysteine.
- Author
- Shearan P; Alvarez JM; Zayed N; Smyth MR
- Address
- School of Chemical Sciences, Dublin City
University, Ireland.
- Source
- Biomed Chromatogr, 1990 Mar, 4:2, 78-82
- Abstract
- An alumina stationary phase has been assessed
in the study of the retention behaviour of the
anticancer drug cisplatin and its major
hydrolysis products. Parameters such as buffer
concentration in the mobile phase, pH, organic
modifier and competing ion have been
investigated in order to optimize
chromatographic separation with ultraviolet
detection. The separation scheme developed has
been used to monitor the hydrolysis of cisplatin
in aqueous and saline media, and to monitor the
interaction of hydrolysed solutions of cisplatin
with the amino acid cysteine. A new peak was
observed in the chromatograms of such mixtures
when they had been allowed to stand for periods
of greater than 16 h and, from analysis of the
data obtained, it was concluded that this new
peak was due to a complex formed between the
mono-aquo hydrolysis product of cisplatin and
the amino acid.
- Language of Publication
- English
- Unique Identifier
- 90275314
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- MeSH Heading (Major)
- Aluminum|*; Aluminum Oxide|*; Chromatography,
High Pressure Liquid|*; Cisplatin|*IP;
Cysteine|*
- MeSH Heading
- Buffers; Cations, Monovalent; Chemistry;
Hydrogen-Ion Concentration; Hydrolysis;
Phosphates; Sodium Chloride; Solutions; Support,
Non-U.S. Gov't; Tetraethylammonium Compounds|PD;
Water
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0269-3879
- Country of Publication
- ENGLAND
Record 10 from database: MEDLINE
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- Title
- Labeling of the beta gamma subunit complex of
transducin with an environmentally sensitive
cysteine reagent. Use of fluorescence
spectroscopy to monitor transducin subunit
interactions.
- Author
- Phillips WJ; Cerione RA
- Address
- Department of Pharmacology, College of
Veterinary Medicine, Cornell University, Ithaca,
New York 14853.
- Source
- J Biol Chem, 1991 Jun, 266:17, 11017-24
- Abstract
- In this study, we have examined the
interactions of the beta gamma subunit complex
of the retinal GTP-binding protein transducin
(beta gamma T) with its alpha subunit (alpha T)
using fluorescence spectroscopic approaches. The
beta gamma T subunit complex was covalently
labeled with
2-(4'-maleimidylanilino)napthalene-6-sulfonic
acid (MIANS), an environmentally sensitive
fluorescent cysteine reagent. The formation of
the MIANS beta gamma T complexes (two to five
MIANS adducts per beta gamma T) resulted in
2-3-fold enhancements in the MIANS fluorescence,
and 20-25-nm blue shifts in the fluorescence
emission maxima, relative to the emission for
identical concentrations of MIANS-labeled MIANS
complexes. The addition of alpha T.GDP to these
MIANS beta gamma T complexes resulted in an
additional enhancement in the MIANS fluorescence
(typically ranging from 20 to 40%) and a 5-10-nm
blue shift in the wavelength for maximum
emission. These fluorescence changes were
specifically elicited by the GDP-bound form of
alpha T and were not observed upon the addition
of purified alpha T.guanosine
5'-O-(3-thiotriphosphate) (GTP gamma S)
complexes to the MIANS beta gamma T species.
Conditions which resulted in the activation of
the alpha T.GDP subunit (i.e. the addition of
AlF4- or the addition of rhodopsin-containing
vesicles and GTP gamma S) resulted in a reversal
of the alpha T.GDP-induced enhancement of the
MIANS beta gamma T fluorescence. Thus the MIANS
beta gamma T fluorescence provided a
spectroscopic monitor for transducin-subunit
association and transducin-activation. Based on
the results from studies using this
spectroscopic read-out, it appears that the
association of the alpha T.GDP species with the
beta gamma T subunit complex to form the
holotransducin molecule is rapid and does not
limit the rate of the rhodopsin-stimulated
activation of holotransducin. However, either
the dissociation of the activated alpha T
subunit from the beta gamma T complex, or a
conformational change in beta gamma T which
occurs as a result of the subunit dissociation
event, appears to be slow relative to the G
protein-subunit association event.
- Language of Publication
- English
- Unique Identifier
- 91250406
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- MeSH Heading (Major)
- Anilino Naphthalenesulfonates|*PD; Cysteine|*;
GTP Phosphohydrolases|*ME; Rod Outer
Segments|*ME; Sulfhydryl Reagents|*PD;
Transducin|IP/*ME
- MeSH Heading
- Aluminum|PD; Animal; Cattle; Fluorine|PD;
Guanosine Diphosphate|ME; Guanosine
5'-O-(3-Thiotriphosphate)|PD; Kinetics;
Macromolecular Systems; Rhodopsin|ME;
Spectrometry, Fluorescence; Support, Non-U.S.
Gov't; Support, U.S. Gov't, Non-P.H.S.; Support,
U.S. Gov't, P.H.S.
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0021-9258
- Country of Publication
- UNITED STATES
Record 11 from database: MEDLINE
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- Title
- Mutations in the nucleotide binding domain of
the alpha subunits of the F1-ATPase from
thermophilic Bacillus PS3 that affect cross-talk
between nucleotide binding sites.
- Author
- Grodsky NB; Dou C; Allison WS
- Address
- Department of Chemistry and Biochemistry,
School of Medicine, University of California,
San Diego, La Jolla 92093-0601, USA.
- Source
- Biochemistry, 1998 Jan, 37:4, 1007-14
- Abstract
- Inactivation of MF1 (bovine mitochondrial
F1-ATPase) with
5'-p-fluorosulfonylbenzoylethenoadenosine is
caused by labeling alpha Y244 [Verburg, J. G.,
and Allison, W. S. (1990) J. Biol. Chem. 265,
8065-8074]. In the crystal structure [Abrahams,
J.P., Leslie, A. G. W., Lutter, R., and Walker,
J. E. (1994) Nature 370, 621-628], alpha Y244 is
hydrogen bonded to alpha R304 which is also
hydrogen bonded to alpha Y300. The catalytic
properties of mutant alpha 3 beta 3 gamma
subcomplexes of the TF1-ATPase from the
thermophilic Bacillus PS3 containing the alpha
F244C, alpha R304C, and alpha Y300C
substitutions have been examined. Each has
unique features for hydrolyzing ATP and forming
inhibitory ADP-fluoroaluminate complexes in
catalytic sites. Unlike wild-type, the (alpha
R304C)3 beta 3 gamma and (alpha Y300C)3 beta 3
gamma subcomplexes entrap inhibitory MgADP in a
catalytic site during turnover which fails to
dissociate when ATP binds to noncatalytic sites.
Although the hydrolytic properties of the (alpha
F244C)3 beta 3 gamma subcomplex and wild-type
are similar, the mutant forms ADP-fluoroaluminate
complexes 7 times faster than wild-type when
Al3+ and F- are added to it in the presence of
excess ADP and Mg2+. It also resists inhibition
by high Mg2+ concentrations in the assay medium.
At least one noncatalytic site of the (alpha
F244C)3 beta 3 gamma subcomplex has increased
affinity for ADP, indicating that the enhanced
rate of formation of the ADP-fluoroaluminate
complex reflects augmented cooperativity between
noncatalytic and catalytic sites. The rate of
formation of the ADP-fluoroaluminate complex in
(alpha Y300C)3 beta 3 gamma increases only 40%
when MgADP in bound to two catalytic sites
rather than one, compared to a 9-fold increase
exhibited by wild type. When Al3+ and F- are
added to the (alpha Y300C)3 beta 3 gamma
subcomplex after incubation with excess ADP and
Mg2+, ADP-fluoroaluminate complexes are formed
in three catalytic sites rather than two
observed with the other subcomplexes.
Reconciliation of the catalytic properties of
the mutant subcomplexes in terms of the crystal
structure suggests that alpha F244, alpha R304,
and alpha Y300 of TF1 are part of a pathway that
propagates conformational signals from one
catalytic site to another.
- Language of Publication
- English
- Unique Identifier
- 98128578
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- MeSH Heading (Major)
- Adenosine Diphosphate|AA/*ME; Adenosine
Triphosphate|*ME; Bacterial Proteins|GE/*ME;
H(+)-Transporting ATP Synthase|GE/*ME
- MeSH Heading
- Aluminum; Arginine|GE; Bacillus|EN; Binding
Sites; Comparative Study; Cysteine|GE; Fluorine;
Hydrolysis; Models, Molecular; Mutagenesis,
Site-Directed; Phenylalanine|GE;
Structure-Activity Relationship; Support, U.S.
Gov't, P.H.S.; Tyrosine|GE
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0006-2960
- Country of Publication
- UNITED STATES
Record 12 from database: MEDLINE
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- Title
- Abiotic factors affecting the toxicity of lead
to fungi.
- Author
- Babich H; Stotzky G
- Address
-
- Source
- Appl Environ Microbiol, 1979 Sep, 38:3, 506-13
- Abstract
- The toxicity of lead (Pb) to fungi in pure
culture was influenced by several abiotic
factors: pH, inorganic anions, clay minerals,
and particulate (humic acid) and soluble organic
matter. The toxicity of Pb was potentiated under
acidic conditions (pH 5 and 6), and phosphate or
carbonate anions reduced the toxicity,
apparently as a result of the formation of
sparingly soluble Pb salts. Clay minerals (montmorillonite
greater than attapulgite greater than kaolinite)
and particulate humic acid protected against the
toxicity of Pb, presumably as the result of
sorption, by cation exchange of the Pb to the
exchange complexes, which reduced its
availability for uptake by the fungi. Soluble
organics, such as tryptone, yeast extract,
cysteine, succinic acid, and increasing
concentrations of neopeptone, also reduced the
toxicity of Pb.
- Language of Publication
- English
- Unique Identifier
- 80128953
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- MeSH Heading (Major)
- Fungi|*DE/GD; Lead|*PD; Soil Microbiology|*
- MeSH Heading
- Aluminum Silicates|PD; Carbonates|PD; Culture
Media; Humic Acids|PD; Hydrogen-Ion
Concentration; Phosphates|PD; Species
Specificity
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0099-2240
- Country of Publication
- UNITED STATES
Record 13 from database: MEDLINE
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- Title
- Comparative inhibition of hepatic
hydroxymethylbilane synthase by both hard and
soft metal cations.
- Author
- Farmer DJ; Hollebone BR
- Address
-
- Source
- Can J Biochem Cell Biol, 1984 Jan, 62:1, 49-54
- Abstract
- The in vitro inhibition of hydroxymethylbilane
synthase (EC 4.3.1.8, uroporphyrinogen I
synthetase) obtained from livers of
Sprague-Dawley rats has been studied with a wide
range of di- and tri-valent metal ions. After
purification by cell lysis, heat treatment, and
centrifugation, the stable, soluble enzyme
yielded sigmoidal inhibition curves with
increasing concentrations of each of the 16 test
ions. Using the negative logarithm of metal
concentration for 50% inhibition (the pM50
value), the metal ions could be classified
according to their Klopman hardness values. Very
soft ions including Hg2+, intermediate ions
including Cr3+, and very hard ions including
Al3+ all yielded large pM50 values indicating
strong inhibition. In comparison to known
metal-ion chemical behaviour, these three ions
could indicate three different types of
inhibitory binding sites at or near the active
site: Hg2+ corresponding to sulfur in cysteine,
Cr3+ corresponding to nitrogen in histidine, and
Al3+ corresponding to oxygen in carboxyl groups.
The presence of the first two sites is also
indicated by the pH dependence of activity.
- Language of Publication
- English
- Unique Identifier
- 84180087
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- MeSH Heading (Major)
- Ammonia-Lyases|*AI; Hydroxymethylbilane
Synthase|*AI; Liver|*EN
- MeSH Heading
- Aluminum|PD; Animal; Cations; Chromium|PD;
Kinetics; Male; Mercury|PD; Rats; Rats, Inbred
Strains
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0714-7511
- Country of Publication
- CANADA
Record 14 from database: MEDLINE
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- Title
- Acute toxicity studies of aluminium compounds:
antidotal efficacy of several chelating agents.
- Author
- Llobet JM; Domingo JL; Gómez M; Tomás JM;
Corbella J
- Address
-
- Source
- Pharmacol Toxicol, 1987 Apr, 60:4, 280-3
- Abstract
- Four aluminum compounds--nitrate, chloride,
sulphate and bromide--were administered orally
and intraperitoneally to rats and mice. The
LD50-values (14 days) were determined. The
majority of deaths occurring during the first
four days. The clinical and physical signs
appearing after intoxication include among other
lethargy, decreased locomotor activity,
piloerection, weight loss and perorbital
bleeding. After 14 days no alterations in liver
and renal functions were detected in the animals
which received intraperitoneally the LD50-values
of aluminum nitrate as a single dose. Aluminum
concentrations were highest in liver and spleen.
No histopathological lesions could be observed.
To compare the efficacies of nine chelating
agents on the toxicity of aluminum in mice, the
therapeutic index and the therapeutic
effectiveness of each chelating agent have been
calculated. Malic, succinic, oxalic and malonic
acids showed the best results with malic and
succinic acids being the most effective.
Deferoxamine mesylate (DFOA), sodium salicylate,
L-cysteine and citric acid were not so effective
as antidotes for acute aluminum toxicity. Aurin
tricarboxylic acid (ATCA) should not be used due
to its high toxicity.
- Language of Publication
- English
- Unique Identifier
- 87231583
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- MeSH Heading (Major)
- Aluminum|AI/*TO; Chelating Agents|*TU
- MeSH Heading
- Animal; Antidotes; Bromides|TO; Chlorides|TO;
Comparative Study; Female; Lethal Dose 50; Male;
Mice; Nitrates|TO; Rats; Rats, Inbred Strains;
Sulfates|TO
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0901-9928
- Country of Publication
- DENMARK
Record 15 from database: MEDLINE
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- Title
- Five genes induced by aluminum in wheat (Triticum
aestivum L.) roots.
- Author
- Snowden KC; Gardner RC
- Address
- Centre for Gene Technology, School of
Biological Sciences, University of Auckland, New
Zealand.
- Source
- Plant Physiol, 1993 Nov, 103:3, 855-61
- Abstract
- Five different cDNAs (termed wali1 to wali5
for Wheat Aluminum Induced) whose expression was
induced by Al stress have been isolated from the
root tips of Al-treated wheat (Triticum aestivum
L.) plants. Four of these genes were induced 24
to 96 h after Al treatment, and their expression
is reduced when the Al is removed. Each of these
four genes was induced by inhibitory levels of
Al in two wheat cultivars--Warigal, an
Al-sensitive cultivar, and Waalt, an Al-tolerant
cultivar. The fifth gene (wali2) showed a
complex bimodal pattern of induction and was
induced by Al only in the sensitive cultivar.
Comparison of the nucleotide sequences of these
clones to those in the sequence data bases
showed that wali4 is homologous to phenylalanine
ammonia-lyase and wali1 is homologous to a group
of plant proteins that are cysteine-rich and
have homology to metallothioneins. wali2 encodes
a novel protein with a repeating motif of
cysteine amino acids. The remaining two wali
clones (wali3 and wali5) encode related,
cysteine-rich proteins that show no significant
homology to any known sequences.
- Language of Publication
- English
- Unique Identifier
- 94294563
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- MeSH Heading (Major)
- Aluminum|*PD; Gene Expression|*DE; Genes,
Plant|*DE; Wheat|DE/*GE/*ME
- MeSH Heading
- Amino Acid Sequence; Base Sequence; Blotting,
Northern; Comparative Study; Consensus Sequence;
Conserved Sequence; DNA|CH/GE; Gene Library;
Molecular Sequence Data; Plants|GE/ME; RNA,
Messenger|AN/BI; Sequence Homology, Amino Acid;
Support, Non-U.S. Gov't
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0032-0889
- Country of Publication
- UNITED STATES
Record 16 from database: MEDLINE
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- Title
- Effect of salts and other agents on
foot-and-mouth disease virus poly (U) polymerase
activity.
- Author
- Polatnick J
- Address
-
- Source
- Arch Virol, 1985, 84:3-4, 269-75
- Abstract
- The activity of the purified poly(U)
polymerase replication complex of foot-and-mouth
disease virus was optimized when 100 mM NH4+ and
either 0.75 mM Al3+ or 1.0 mM Fe3+ was added to
the standard assay reaction mixture. Zn2+ at
concentrations of 10(-5) mM to 5 mM inhibited
enzyme activity although all polymerases
examined to date have contained zinc.
Mercaptoethanol and dithiothreitol inhibited
polymerase activity despite the presence of
cysteine residues in the viral induced
polypeptide of the replication complex, possibly
because of their action as metal chelators
rather than as reducing agents.
- Language of Publication
- English
- Unique Identifier
- 85198398
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- MeSH Heading (Major)
- Aphthovirus|*EN; Nucleotidyltransferases|AI/*ME
- MeSH Heading
- Aluminum|PD; Ammonium Chloride|PD;
Dithiothreitol|PD; Ethylmaleimide|PD; Ferric
Compounds|PD; Mercaptoethanol|PD; Metals|PD;
Oxidation-Reduction; Zinc|PD
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0304-8608
- Country of Publication
- AUSTRIA
Record 17 from database: MEDLINE
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- Title
- Oxidation of the
alpha(3)(betaD311C/R333C)(3)gamma subcomplex of
the thermophilic Bacillus PS3 F(1)-ATPase
indicates that only two beta subunits can exist
in the closed conformation simultaneously.
- Author
- Ren H; Dou C; Stelzer MS; Allison WS
- Address
- Department of Chemistry, University of
California at San Diego, La Jolla, California
92093-0506, USA.
- Source
- J Biol Chem, 1999 Oct, 274:44, 31366-72
- Abstract
- In the crystal structure of the bovine heart
mitochondrial F(1)-ATPase (Abrahams, J. P.,
Leslie, A. G. W., Lutter, R., and Walker, J. E.
(1994) Nature 370, 621-628), the two liganded
beta subunits, one with MgAMP-PNP bound to the
catalytic site (beta(T)) and the other with
MgADP bound (beta(D)) have closed conformations.
The empty beta subunit (beta(E)) has an open
conformation. In beta(T) and beta(D), the
distance between the carboxylate of
beta-Asp(315) and the guanidinium of
beta-Arg(337) is 3.0-4.0 A. These side chains
are at least 10 A apart in beta(E). The
alpha(3)(betaD311C/R333C)(3)gamma subcomplex of
TF(1) with the corresponding residues
substituted with cysteine has very low ATPase
activity unless it is reduced prior to assay or
assayed in the presence of dithiothreitol. The
reduced subcomplex hydrolyzes ATP at 50% the
rate of wild-type and is rapidly inactivated by
oxidation by CuCl(2) with or without magnesium
nucleotides bound to catalytic sites. Titration
of the subcomplex with iodo[(14)C]acetamide
after prolonged treatment with CuCl(2) in the
presence or absence of 1 mM MgADP revealed
nearly two free sulfhydryl groups/mol of enzyme.
Therefore, one pair of introduced cysteines is
located on a beta subunit that exists in the
open or partially open conformation even when
catalytic sites are saturated with MgADP. Since
V(max) of ATP hydrolysis is attained when three
catalytic sites of F(1) are saturated, the
catalytic site that binds ATP must be closing as
the catalytic site that releases products is
opening.
- Language of Publication
- English
- Unique Identifier
- 20002663
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- MeSH Heading (Major)
- Bacillus|*EN; H(+)-Transporting ATP Synthase|*CH/GE/ME
- MeSH Heading
- Adenosine Triphosphate|ME; Adenylyl
Imidodiphosphate|ME; Aluminum|PD; Copper|PD;
Dithiothreitol|PD; Edetic Acid|PD; Fluorine|PD;
Heat; Hydrolysis; Iodoacetamide|PD;
Iodoacetates|PD; Models, Molecular; Mutagenesis;
Oxidation-Reduction; Protein Conformation;
Protein Structure, Quaternary; Support, U.S.
Gov't, P.H.S.
- Publication Type
- JOURNAL ARTICLE
- ISSN
- 0021-9258
- Country of Publication
- UNITED STATES
Record 18 from database: MEDLINE
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- Title
- Five genes induced by aluminum in wheat (Triticum
aestivum L.) roots.
- Author
- Snowden KC; Gardner RC
- Address
- Centre for Gene Technology, School of
Biological Sciences, University of Auckland, New
Zealand.
- Source
- Plant Physiol, 1993 Nov, 103:3, 855-61
- Abstract
- Five different cDNAs (termed wali1 to wali5
for Wheat Aluminum Induced) whose expression was
induced by Al stress have been isolated from the
root tips of Al-treated wheat (Triticum aestivum
L.) plants. Four of these genes were induced 24
to 96 h after Al treatment, and their expression
is reduced when the Al is removed. Each of these
four genes was induced by inhibitory levels of
Al in two wheat cultivars--Warigal, an
Al-sensitive cultivar, and Waalt, an Al-tolerant
cultivar. The fifth gene (wali2) showed a
complex bimodal pattern of induction and was
induced by Al only in the sensitive cultivar.
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