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Amino Acid Sequence Homology between Pig Heart Lipoamide Dehydrogenase and Human Erythrocyte Glutathione Reductase

Charles H. Williams, L. David Arscott and Georg E. Schulz
Proceedings of the National Academy of Sciences of the United States of America
Vol. 79, No. 7, [Part 1: Biological Sciences] (Apr. 1, 1982), pp. 2199-2201
Stable URL: http://www.jstor.org/stable/11595
Page Count: 3
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Amino Acid Sequence Homology between Pig Heart Lipoamide Dehydrogenase and Human Erythrocyte Glutathione Reductase
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Abstract

Extensive amino acid sequence homology has been found between nine tryptic peptides of pig heart lipoamide dehydrogenase [NADH:lipoamide oxidoreductase, EC 1.6.4.3] and the sequence of human erythrocyte glutathione reductase [NAD(P)H:glutathione oxidoreductase, EC 1.6.4.2]. The average homology is 40%. Six lipoamide dehydrogenase peptides are homologous with segments of the two parts of the FAD domain of glutathione reductase, one with the NADPH domain, and two with the interface domain. Thus, the homology extends throughout the molecule.

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