GLUTATHIONE-REDUCTASE FROM HUMAN-ERYTHROCYTES - AMINO-ACID-SEQUENCE OF A MAJOR FRAGMENT THAT LINKS THE FAD, NADP AND INTERFACE DOMAINS

被引：15

作者：

SCHILTZ, E ^{[1
]}

BLATTERSPIEL, R ^{[1
]}

UNTUCHTGRAU, R ^{[1
]}

机构：

[1] MAX PLANCK INST MED RES,D-6900 HEIDELBERG,FED REP GER

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 102卷 / 01期

关键词：

D O I：

10.1111/j.1432-1033.1979.tb06289.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：269 / 278

页数：10

共 20 条

[1] INHIBITION OF PROTEIN-SYNTHESIS INITIATION BY OXIDIZED GLUTATHIONE - ACTIVATION OF A PROTEIN-KINASE THAT PHOSPHORYLATES ALPHA-SUBUNIT OF EUKARYOTIC INITIATION FACTOR-2 [J].