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A Cassaigne

Publications and source records attributed to A Cassaigne.

At least 37 records · Page 2Linked to original sources
PubMed1990

Genotyping study of alcohol dehydrogenase class I polymorphism in French patients with alcoholic cirrhosis. The French Group for Research on Alcohol and Liver.

Comparison of alcohol dehydrogenase polymorphism at the loci ADH2 and ADH3 is made in France between 46 alcoholic cirrhotic patients and 39 controls, by genotyping technique using polymerase chain reaction on blood microsample collected on blotting paper. The genotype distributions are similar, with low frequency of the ADH2(2) allele. Polymorphism at the ADH3 locus is not a genetic factor for alcoholic cirrhosis in France.

Adult↗
PubMed1989

Phosphonoacetaldehyde hydrolase from Pseudomonas aeruginosa: purification properties and comparison with Bacillus cereus enzyme.

Phosphonoacetaldehyde hydrolase (2-oxoethylphosphonate phosphonohydrolase, EC 3.11.1.1) has been purified to electrophoretic homogeneity from cells of Pseudomonas aeruginosa A 237 grown in a culture medium containing 2-aminoethylphosphonate as both phosphorus and carbon sources. The native Mr has been estimated to be 62,000 +/- 2000, using a gel filtration column equilibrated with standard proteins. A subunit of Mr 30,000 +/- 1000 determined in sodium dodecyl sulfate-polyacrylamide gel electrophoresis gives evidence of a homodimeric structure. The enzyme, which catalyzes the C-P bond cleavage of phosphonoacetaldehyde, has a Km value of 210 microM. It is moderately inhibited by methyl-, ethyl-, propyl- and butylphosphonic acids and activated by aminomethyl-, aminoethylphosphonic acids as well as by phosphonoformic, phosphonoacetic and phosphonopropionic acids. Inhibition by orthophosphite is a time-dependent process which exhibits first-order kinetics and is enhanced by the presence of acetaldehyde. Assays for phosphite removal by dilution or dialysis do not reverse the inhibition. Phosphonoacetaldehyde hydrolase inactivation by phosphite ion appears to be inconsistent with the concept of a Schiff base intermediate as proposed for Bacillus cereus enzyme.

Bacillus cereus↗
PubMed1987

Interaction of phosphonates related to glutathione with the rat kidney gamma-glutamylcysteine synthetase.

Various phosphonic and sulfonic glutamate analogues as well as phosphonopeptides related to glutathione were studied for their interaction with rat kidney gamma-glutamylcysteine synthetase activity. We found, in all cases, that the presence of a phosphonic group increases the affinity for the enzyme. Among the tripeptides tested, the phosphonic analogue of ophthalmic acid (gamma Glu-Abu-Gly-P) is the most potent inhibitor. The glutamate and cysteine sites of the enzyme seem to be involved in the binding of this compound, since either substrate protects against inhibition. The types of inhibition with respect to the different substrates show dissimilar behaviors of the tripeptides, in spite of their structural analogy. Investigations relative to the role of the divalent ion Mg2+ provided evidence that the actual inhibitors are Mg2+-tripeptide complexes for the phosphonic compounds, whereas chelation with a metal ion is not required for inhibition by glutathione.

Animals↗
PubMed1985

Effect of phosphonic analogues of glutamic acid on glutamate decarboxylase.

Among the phosphonic analogues of glutamic acid, only 4-amino-4-phosphono butyric acid, the compound which shows the highest affinity for pyridoxal phosphate, inhibits competitively both Escherichia coli and rat brain glutamate decarboxylases. Phosphinothricin, 2-amino-4-(methylphosphino)butyric acid, is a strong inhibitor of the mammalian enzyme.

Animals↗
PubMed1983

Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa.

2-Aminoethylphosphonate aminotransferase has been purified to homogeneity with a yield of 15% from cell extracts of Pseudomonas aeruginosa. The molecular weight of the enzyme was estimated by gel filtration to be 65000 +/- 2000. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis yielded a molecular weight of 16500 +/- 1000, suggesting a tetrameric model for this protein. The absorption spectrum exhibits maxima at 280 nm, 335 nm and 415 nm which are characteristic of a pyridoxal-phosphate-dependent enzyme: 4 mol of pyridoxal 5'-phosphate/mol of enzyme have been found. This aminotransferase catalyzes the transfer of the amino group of 2-aminoethylphosphonate (ciliatine) to pyruvate to give 2-phosphonoacetaldehyde and alanine. A pH optimum between 8.5-9 and an activity increasing from 30 degrees C to 50 degrees C have been observed. The reaction follows Michaelis-Menten kinetics with Km values of 3.85 mM and 3.5 mM for ciliatine and pyruvate respectively. This enzyme shows a very high specificity since ciliatine and pyruvate are the only amino donor and acceptor respectively. Methyl, ethyl and propylphosphonic acids are better competitors towards ciliatine than their alpha-amino derivatives. 3-Aminopropylphosphonate, the higher homologue of ciliatine, is recognized neither as a substrate nor as an inhibitor. The enzyme activity is significantly affected by carbonyl reagents and by HgCl2. Transamination of 2-aminoethylphosphonate is the first step of a double-step pathway which leads to the cleavage of its C-P bond.

Hydrogen-Ion Concentration↗
PubMed1982

[Opioid peptides].

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Amino Acid Sequence↗
PubMed1976

[2-Amino-ethylphosphonic acid transport in Pseudomonas aeruginosa].

2-Aminoethylphosphonic acid (ciliatine) can be used as a source of phosphorus or nitrogen by Pseudomonas aeruginosa. The conditions of its uptake have been investigated. The transport is inducible by ciliatine itself or by its homologue, 3-aminopropylphosphonate, but neither by other phosphonic compounds nor by carboxylic or sulfonic related derivatives. The induction was not suppressed by inorganic phosphate. The transport appears to be an active process, pH and temperature dependent: it requires energy and is dependent on new protein synthesis. The uptake follows Michaelis kinetics. The substrate specificity involved in ciliatine uptake favours the existence of two different transport systems: the first one, inducible by ciliatine, was very sensitive towards different aminophosphonic acids and was competitively inhibited by inorganic phosphate and methylphosphonate; the second transport system, inducible by 3-amino-propylphosphonate, appeared less sensitive towards alpha-aminophosphonic acids and was non competitively inhibited by phosphate and methylphosphonate. No interactions were observed with related aminocarboxylic acids or with taurine. Some molecular structural requirements for the binding of an effector on both permeases are discussed. The regulatory function of inorganic phosphate, the chief breakdown product of ciliatine, is also emphasized.

Aminoethylphosphonic Acid↗
PubMed1975

In vivo incorporation of cytidine-monophosphate-ciliatine into rat liver lipids.

1. In vivo this investigation was carried out in order to compare the incorporation into rat lipids of free [1,2-minus 14C]-ciliatine and CMP-[1,2-minus 14C]-ciliatine which is the precursor in phosphonolipid biosynthesis. 2. The incorporation of the radioactivity from CMP-[1,2-minus 14C]-ciliatine took place more rapidly than that from free [1,2-minus 14C]-ciliatine in both liver and kidney. The amount of radioactivity from the CMP-[1,2-minus 14C]-ciliatine incorporated into total liver lipids was about 5 times higher than that incorporated into total liver lipids of rat two hrs after injecting free-[1,2-minus 14C]-ciliatine. 3. The amount of [1,2-minus 14C]-ciliatine incorporated into total liver lipids was 15 and 21 times higher than that incorporated into total kidney lipids of rat two and four hrs after injecting free [1,2-minus 14C]-ciliatine. 4. If the main pathway for the phosphonolipid biosynthesis is via CMP-ciliatine, the rate of phosphonolipid formation from CMP-ciliatine must therefore be higher than that from free-ciliatine. The results obtained here indicate therefore that the main pathway for phosphonolipid biosynthesis is a pathway involving CMP-ciliatine. 5. An unknow compound was detected in the water soluble fraction of the acid hydrolyzate of liver phosphonolipids. This material migrated with the N-trimethyl-derivative of ciliatine on the thin-layer chromatogram. The result shows that there is therefore a possibility of methylation of exogenous ciliatine to the phosphonate analogue of choline in the mammalian body.

Aminoethylphosphonic Acid↗