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Amino acid sequence of human muscle glyceraldehyde-3-phosphate dehydrogenase. Isolation and amino acid sequences of tryptic peptides.

作者信息

Nowak K, Malarska A, Ostropolska L, Kuczek M, Zowmir O, Slomińska A, Wolny M, Baranowski T

出版信息

Acta Biochim Pol. 1976;23(2-3):127-38.

PMID:987679
Abstract
  1. The amino acid compostion, N- and C-terminal amino acid sequences, and the subunit molecular weight of glyceraldehyde phosphate dehydrogenase from human muscle, were determined. The obtained results and the maps of tryptic peptides suggest that the enzyme is composed of four identical or very similar polypeptide chains. 2. From the tryptic digest of performic acid-oxidized enzyme, 32 peptides were isolated. The amino acid sequence analysis showed a high degree of homology with the corresponding tryptic peptides of the dehydrogenase from pig muscle, with 9 replacements and probably two additional amino acids in the examined sequences of the human muscle enzyme.
摘要

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A structural study of pig liver glyceraldehyde-3-phosphate dehydrogenase.
Biochim Biophys Acta. 1976 Jul 19;439(1):38-46. doi: 10.1016/0005-2795(76)90157-4.

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