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Your search keyword '"Francis DeToma"' showing total 3 results
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3 results on '"Francis DeToma"'

1. Active site peptides of rhodanese

Author

John Westley and Francis DeToma

Subjects
Electrophoresis, Paper, Chromatography, Gas, Cyanide, Thiosulfates, Sulfurtransferase, Iodoacetates, Peptide, Rhodanese, Biochemistry, Genetics and Molecular Biology (miscellaneous), chemistry.chemical_compound, Column chromatography, Transferases, Trypsin, Cysteine, Amino acid residue, Thiosulfate, chemistry.chemical_classification, Carbon Isotopes, Chromatography, Binding Sites, Cyanides, biology, Tryptophan, Active site, Biochemistry, chemistry, biology.protein, Peptides
Abstract

The active site cysteinyl peptide isolated from a tryptic digest of rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1) by column chromatography has been found to contain 15 amino acid residues, of which 7 are hydrophobic. The tryptophyl peptides in such digests also appear to consist predominantly of residues which are hydrophobic.

Published
1970

2. Dimeric structure and zinc content of bovine liver rhodanese

Author

John Westley, Francis DeToma, and Marguerite Volini

Subjects
Electrophoresis, Chemical Phenomena, Protein Hydrolysates, Metal ions in aqueous solution, Dimer, Inorganic chemistry, Size-exclusion chromatography, chemistry.chemical_element, Zinc, Rhodanese, Biochemistry, chemistry.chemical_compound, Transferases, Polymer chemistry, Native state, Animals, Molecular Biology, chemistry.chemical_classification, Chemistry, Physical, Cell Biology, Hydrogen-Ion Concentration, Centrifugation, Zonal, Molecular Weight, Monomer, Enzyme, chemistry, Liver, Models, Chemical, Chromatography, Gel, Cattle, Peptides, Oxidation-Reduction, Polarography
Abstract

Evidence from gel filtration and sedimentation studies of crystalline bovine liver rhodanese indicated that the enzyme molecule of 37,000 molecular weight is a dimer. In the native state, this form is in rapid, pH-dependent equilibrium with the monomeric species. A stable dimer is formed under mild oxidizing conditions. Analysis of the protein by peptide mapping indicated that the monomers are identical. Polarographic analysis for metal ions showed that the enzyme contains 1 zinc ion per monomer.

Published
1967

3. Improved Preparation of Bovine Liver Rhodanese

Author

Paul M. Horowitz and Francis DeToma

Subjects
Chromatography, Biochemistry, Chemistry, Yield (chemistry), Liver tissue, Cell Biology, Rhodanese, Molecular Biology, Thiosulfate sulfurtransferase
Abstract

A better method for isolating crystalline rhodanese from bovine liver tissue has been developed. Both the improved over-all yield of enzymic activity obtained and the ease with which the procedure can be carried out make this the method of choice for large scale preparations.

Published
1970

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