PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR PROTEINASE FROM BREVIBACTERIUM-LINENS ATCC-9174

被引：47

作者：

RATTRAY, FP ^{[1
]}

BOCKELMANN, W ^{[1
]}

FOX, PF ^{[1
]}

机构：

[1] BUNDESANSTALT MILCHFORSCH,INST MIKROBIOL,W-2300 KIEL,GERMANY

来源：

APPLIED AND ENVIRONMENTAL MICROBIOLOGY | 1995年 / 61卷 / 09期

关键词：

D O I：

10.1128/AEM.61.9.3454-3456.1995

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

An extracellular serine proteinase from Brevibacterium linens ATCC 9174 was purified to homogeneity. pH and temperature optima were 8,5 and 50 degrees C, respectively. The results for the molecular mass of the proteinase were 56 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 126 kDa by gel filtration, indicating that the native enzyme exists as a dimer. Mg2+ and Ca2+ activated the proteinase, as did NaCl; however, Hg2+ Fe2+, and Zn2+ caused strong inhibition. The sequence of the first 20 N-terminal amino acids was NH2-Ala-Lys-Asn-Asp-Ala-Val-Gly-Gly-Met-Gly-Tyr-Leu-Ser-Met-IIe-Pro-Ser-Gln-Pro-Gly.

引用

页码：3454 / 3456

页数：3

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