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PMID: 7417521 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Glutathione reductase activity and pyridoxine (pyridoxamine) phosphate oxidase activity in the red cell.

Biochimica et biophysica acta ·Vol. 632 ·No. 2 ·1980-10-01 ·Pages 159-63

Clements JE, Anderson BB

Abstract

The red-cell enzymes, glutathione reductase (FAD-dependent) and pyridoxine (pyridoxamine) phosphate oxidase (FMN-dependent), were studied in control subjects. The wide range in the glutathione reductase activity correlated inversely with the percentage stimulation by FAD added in vitro, and with pyridoxine (pyridoxamine) phosphate oxidase activity. Both enzymes were stimulated after ingestion of riboflavin. The results support the suggestion that the rate of metabolism of riboflavin in the red cell controls the activity of both enzymes, and the rate of red-cell metabolism of vitamin B-6.

MeSH Terms
Erythrocytes/enzymology Flavin-Adenine Dinucleotide/pharmacology Glutathione Reductase/blood Humans Kinetics Oxidoreductases Acting on CH-NH Group Donors/blood Pyridoxaminephosphate Oxidase/blood Pyridoxine/blood Riboflavin/blood,pharmacology
Chemicals
Flavin-Adenine Dinucleotide Pyridoxaminephosphate Oxidase Oxidoreductases Acting on CH-NH Group Donors Glutathione Reductase Pyridoxine Riboflavin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Clements J E
Anderson B B
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1980-10-01
Pages
159-63
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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