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

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.

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EurJBiochem_102_1979_269.pdf (Any fulltext), 679KB
 
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SCHILTZ , Emil, Author
BLATTERSPIEL , Rosi, Author
Untucht-Grau, Renate1, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 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.

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Language(s): eng - English
 Dates: 1979-07-262008-06-281979-12
 Publication Status: Published in print
 Pages: 10
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 Rev. Type: Peer
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 102 (1) Sequence Number: - Start / End Page: 269 - 278 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040