PRIMARY STRUCTURE OF THE INORGANIC PYROPHOSPHATASE FROM THERMOPHILIC BACTERIUM PS-3

被引:28
作者
ICHIBA, T
TAKENAKA, O
SAMEJIMA, T
HACHIMORI, A
机构
[1] SHINSHU UNIV,FAC TEXT SCI & TECHNOL,INST HIGH POLYMER RES,UEDA,NAGANO 386,JAPAN
[2] KYOTO UNIV,PRIMATE RES INST,DEPT BIOCHEM,INUYAMA,AICHI 484,JAPAN
[3] AOYAMA GAKUIN UNIV,COLL SCI & ENGN,DEPT CHEM,SETAGAYA KU,TOKYO 157,JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a123244
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
The complete amino acid sequence of the inorganic pyrophosphatase from thermophilic bacterium PS-3 was determined by automated Edman analysis of the intact protein and of peptides derived from digests obtained with lysylendopeptidase, Staphylococcus aureus strain V8 protease, and arginylendopeptidase. The monomer peptide chain comprises 164 amino acid residues and has a calculated molecular weight of 18,792. The sequence is identical at about 46% of the amino acid positions with that of the Escherichia coli enzymes. © 1990 Copyright, 1990 by the Journal of Biochemistry.
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页码:572 / 578
页数:7
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