Amino acid sequence of penicillopepsin. I. Isolation and characterization of the chymotryptic peptides.
Amino acid sequence of penicillopepsin. I. Isolation and characterization of the chymotryptic peptides.
复制标题
青霉蛋白酶的氨基酸序列。
DOI：
10.1139/o76-125
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发表时间：
1976
期刊：
影响因子：
--
通讯作者：
T. Hofmann
中科院分区：
文献类型：
--
作者：
A. Kurosky;T. Hofmann
已确定从霉菌酸性蛋白酶青霉蛋白酶 (EC 3.4.23.7) 的胰凝乳蛋白酶消化中获得的 48 种肽的氨基酸序列。这些肽建立了 26 个独特片段的序列，长度最多为 28 个残基。 28 个残基片段被鉴定为 N 末端区域。 C 末端区域由 13 个残基片段表示。这些片段中所含的氨基酸约占酶残基的 85%。
The amino acid sequences of 48 peptides obtained from a chymotryptic digest of the mould acid protease, penicillopepsin (EC 3.4.23.7), have been determined. These peptides established the sequences of 26 unique fragments of up to 28 residues in length. The 28-residue fragment was identified as the N-terminal region. The C terminal region is represented by a 13-residue fragment. The amino acids contained in these fragments account for some 85% of the residues of the enzyme.