PURIFICATION OF 3 SERINE PROTEASES FROM THE CELOMIC CELLS OF EARTHWORMS (EISENIA-FOETIDA)

被引：27

作者：

ROCH, P ^{[1
]}

STABILI, L ^{[1
]}

PAGLIARA, P ^{[1
]}

机构：

[1] UNIV LECCE,DIPARTMENTO BIOL,I-73100 LECCE,ITALY

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1991年 / 98卷 / 04期

关键词：

D O I：

10.1016/0305-0491(91)90261-B

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：

1. Proteinase activity is evidenced in coelomic cell lysate of Eisenia fetida andrei. 2. Tested on gelatin plates, the proteolysis developes rapidly during the first hr of incubation at 37-degrees-C. 3. The proteolysis is pH-dependent with two optima for pH 7.0 and 10.0. 4. The proteolysis is dose-dependent. 5. The proteolysis is not influenced by ionic strenght. 6. The proteolysis is thermo-sensitive but not totally suppressed by 15 min at 100-degrees-C. 7. Three serine proteases, A2 (M(r) 42kDa), B2 (M(r) 46kDa) and C2 (M(r) 48kDa), were purified by affinity chromatography on benzamidine-Sepharose. 8. According to various inhibition and activity tests, A2 is of trypsin-like type, Ca2+-independent but Mg2+- and Mn2+-dependent and C2 is of chymotrypsin-like type.

引用

页码：597 / 602

页数：6

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