Open AccessGlutathione Reductase from Human Erythrocytes
Author(s) -
SCHILTZ Emil,
BLATTERSPIEL Rosi,
UNTUCHTGRAU Renate
Publication year - 1979
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1979.tb06289.x
Subject(s) - thermolysin , edman degradation , trypsin , peptide , chymotrypsin , peptide sequence , chemistry , biochemistry , amino acid , sequence (biology) , glutathione reductase , glutathione , enzyme , stereochemistry , glutathione peroxidase , gene
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.