PURIFICATION AND CHARACTERIZATION OF A NOVEL TRIPEPTIDYL AMINOPEPTIDASE FROM STREPTOMYCES-LIVIDANS-66

被引：18

作者：

KRIEGER, TJ ^{[1
]}

BARTFELD, D ^{[1
]}

JENISH, DL ^{[1
]}

HADARY, D ^{[1
]}

机构：

[1] CANGENE CORP,MISSISSAUGA L4V 1J7,ON,CANADA

来源：

FEBS LETTERS | 1994年 / 352卷 / 03期

关键词：

TRIPEPTIDYL AMINOPEPTIDASE; RECOMBINANT PROTEIN EXPRESSION; PROTEIN DEGRADATION; SERINE PROTEINASE; FERMENTATION; STREPTOMYCES LIVIDANS;

D O I：

10.1016/0014-5793(94)00988-0

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：

An extracellular tripeptidyl aminopeptidase has been purified from Streptomyces lividans 66 cell-free cultures. The enzyme is a major component of the secreted proteolytic activity. The protease removes only the N-terminal tripeptide from recombinant human GM-CSF and IL-3 but does not cleave recombinant human IL-6. The enzyme cleaves the synthetic tripeptide substrates APA-pNA and APM-pNA but does not cleave substrates with blocked amino terminals. Smaller substrates are not cleaved. The enzyme appears to be a serine protease of 55 kDa molecular weight. The pH optimum is between 7.5 and 8.5 but varies slightly with the substrate. The N-terminal sequence and amino acid composition have been determined.

引用

页码：385 / 388

页数：4

共 22 条

[1] PURIFICATION AND PROPERTIES OF AN EXTRACELLULAR AMINOPEPTIDASE FROM STREPTOMYCES-LIVIDANS 1326 [J].