Glutathione reductase from human erythrocytes amino‐acid sequence of a major 
fragment that links the FAD, NADP and interface domains

SCHILTZ , Emil; BLATTERSPIEL , Rosi; Untucht-Grau, Renate

doi:10.1111/j.1432-1033.1979.tb06289.x

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Glutathione reductase from human erythrocytes amino‐acid sequence of a major fragment that links the FAD, NADP and interface domains

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Untucht-Grau, Renate
Max Planck Institute for Medical Research, Max Planck Society;

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SCHILTZ, E., BLATTERSPIEL, R., & Untucht-Grau, R. (1979). Glutathione reductase from human erythrocytes amino‐acid sequence of a major fragment that links the FAD, NADP and interface domains. European Journal of Biochemistry, 102(1), 269-278. doi:10.1111/j.1432-1033.1979.tb06289.x.

Cite as: https://hdl.handle.net/21.11116/0000-0004-4D81-4

Abstract

A major CNBr fragment of glutathione reductase, peptide Q [Krohne‐Ehrich, G., Schirmer, R. H. & Untucht‐Grau, R. (1977) Eur. J. Biochem. 80, 65–71], was further fractionated by trypsin, chymotrypsin, thermolysin and clostripain digestion. The peptides were isolated and most of them were sequenced by solid‐phase Edman degradation. The whole peptide Q was sequenced N‐terminally up to position 51 by the same technique. A total sequence of 128 amino acids (28% of the whole protein) was obtained and could be localized in the electron density map [Schulz, G. E., Schirmer, R. H., Sachsenheimer, W. & Pai, E. F. (1978) Nature (Lond.) 273, 120–124] from position 259–387. This part of the polypeptide links and participates in all three domains of the flavoenzyme.