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Biomedical subjects

C Anthony

Publications and source records attributed to C Anthony.

101 records · Page 6Linked to original sources
PubMed1967

The microbial oxidation of methanol. Purification and properties of the alcohol dehydrogenase of Pseudomonas sp. M27.

1. A method for the purification of the nicotinamide nucleotide-independent alcohol dehydrogenase of Pseudomonas sp. M27 is described. 2. In the analytical ultracentrifuge, the purified enzyme shows a single major component of molecular weight 146000. 3. On electrophoresis in polyacrylamide gels between pH5.0 and 9.55, it shows only one protein band and the isoelectric point appears to be between pH7.0 and 8.0. 4. Spectrographic analysis indicates no significant metal content. 5. Amino acid analysis shows an unusually small number of cysteine/cystine residues per molecule as well as about 4.1% of glucosamine. 6. The role of ammonia as enzyme activator has been investigated.

Alcohol Oxidoreductases↗
PubMed1967

The microbial oxidation of methanol. The prosthetic group of the alcohol dehydrogenase of Pseudomonas sp. M27: a new oxidoreductase prosthetic group.

1. The purified alcohol dehydrogenase of Pseudomonas sp. M27, whose action is independent of nicotinamide nucleotides, has absorption peaks at 280mmu and at 350mmu with little or no absorption at or above 450mmu. 2. It does not fluoresce, but green-fluorescent material, diffusible on dialysis, is produced when the enzyme is treated with acid or alkali or when it is boiled. 3. Evidence is presented that the enzyme is not a flavoprotein. 4. Kinetic studies show a correlation between enzyme inactivation by acid, alkali or heat and liberation of the fluorescent material. 5. Some purification of the fluorescent material was achieved, but definite identification was not possible; the major component has a fluorescence maximum at about 460mmu with excitation maxima at about 260mmu and 365mmu. 6. Data are given (including absorption and fluorescence spectra) that support the suggestion that the prosthetic group of the enzyme is a pteridine derivative. 7. Possible mechanisms of action of the enzyme are discussed.

Alcohol Oxidoreductases↗
PubMed1965

The microbial oxidation of methanol. The alcohol dehydrogenase of Pseudomonas sp. M27.

1. No primary hydrogen acceptor other than phenazine methosulphate has been found for the alcohol dehydrogenase from Pseudomonas sp. M27. 2. None of a wide range of vitamins or cofactors has any effect on the activity of the enzyme. 3. The enzyme is far less sensitive to metal-chelating agents and thiol reagents than are other alcohol dehydrogenases. 4. Methanol is oxidized at least as fast as other alcohols by this enzyme and its well-defined substrate specificity is different from that of other alcohol dehydrogenases. Only primary alcohols are oxidized; the general formula for an oxidizable substrate is R.CH(2).OH, where R may be H or [Formula: see text] 5. Whole organisms oxidize only those alcohols that are oxidized by the isolated enzyme.

Alcohol Oxidoreductases↗