MEMBRANE ACETYLCHOLINESTERASE FROM APIS-MELLIFERA HEAD SOLUBILIZED BY PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C INTERACTS WITH AN ANTI-CRD ANTIBODY

被引：13

作者：

BELZUNCES, LP

THEVENIAU, M

MASSON, P

BOUNIAS, M

机构：

[1] SERV SANTE ARMEES,CTR RECH,UNITE BIOCHIM,F-38700 LA TRONCHE,FRANCE

[2] UNIV AIX MARSEILLE 1,INST CHIM BIOL,F-13331 MARSEILLE 3,FRANCE

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1990年 / 95卷 / 03期

关键词：

D O I：

10.1016/0305-0491(90)90029-S

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. 1. Membrane acetylcholinesterase from Apis mellifera head was solubilized by a phosphatidylinositol specific phospholipase C (PI-PLC) from Bacillus thuringiensis in a dose-dependent mode. 2. 2. The PI-PLC cleavage product is a hydrophilic form with an increased electrophotetic mobility which binds to an anti-cross-reaching determinant (CRD) antibody. © 1990.

引用

页码：609 / 612

页数：4

共 27 条

[1] ARRHENIUS PLOTS OF ACETYLCHOLINESTERASE ACTIVITY IN MAMMALIAN ERYTHROCYTES AND IN TORPEDO ELECTRIC ORGAN - EFFECT OF SOLUBILIZATION BY PROTEINASES AND BY A PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C [J].