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Your search keyword '"Nancy A. Avedovech"' showing total 2 results
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2 results on '"Nancy A. Avedovech"'

1. Mammalian hypotaurine aminotransferase: Isethionate is not a product

Author

Kermit D. McCarthy, J. H. Fellman, Esther S. Roth, and Nancy A. Avedovech

Subjects
Alkanesulfonates, Taurine, Transamination, Isethionic Acid, Hypotaurine, Acetaldehyde, Biology, General Biochemistry, Genetics and Molecular Biology, Mice, chemistry.chemical_compound, Hypotaurine aminotransferase, Animals, Germ-Free Life, Tissue Distribution, General Pharmacology, Toxicology and Pharmaceutics, Transaminases, chemistry.chemical_classification, Isethionic acid, General Medicine, In vitro, Rats, Models, Chemical, chemistry, Biochemistry, Sulfinoacetaldehyde, Aminotransferase activity
Abstract

We report that mammalian tissues posses hypotaurine (2-aminoethane- sulfinate) aminotransferase activity. One product of transamination, sulfinoacetaldehyde could theoretically undergo internal oxidation-reduction leading to isethionate (2-hydroxyethanesulfonate). This hypothesis was examined. No isethionate was formed in vitro .

Published
1980
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2. Cysteine thiosulfonate in cystine metabolism

Author

Jack H. Fellman and Nancy A. Avedovech

Subjects
chemistry.chemical_classification, Male, biology, Chemistry, Biophysics, Cystine, Rats, Inbred Strains, Metabolism, Cleavage (embryo), Biochemistry, Cystathionine beta synthase, In vitro, Amino acid, Diet, Rats, chemistry.chemical_compound, Liver, In vivo, biology.protein, Animals, Cysteine, Molecular Biology
Abstract

A sulfur-containing amino acid was observed in mammalian cystine metabolism, in vitro and in vivo , which we have characterized as 2-amino, 3-(thio-thiosulfonate)propionic acid (cysteine thiosulfonate). Its biosynthetic pathway appears to initiate with the cleavage of cystine by cystathionine γ-lyase to form thiocystine, which undergoes sulfinolysis to form cysteine thiosulfonate.

Published
1982

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