LOCALIZATION OF 2 GLYCOLYTIC-ENZYMES IN GUINEA-PIG TAENIA-COLI

被引：10

作者：

HARDIN, CD ^{[1
]}

PAUL, RJ ^{[1
]}

机构：

[1] UNIV CINCINNATI,DEPT PHYSIOL & BIOPHYS,CINCINNATI,OH 45221

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1134卷 / 03期

关键词：

GLYCOLYSIS; SMOOTH MUSCLE; ENZYME LOCALIZATION; (T-COLI);

D O I：

10.1016/0167-4889(92)90184-D

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：

The bound fractions of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and of fructose 1,6-diphosphate aldolase (ALD) were measured in intact Taenia coli. ALD was approximately 60% bound and GAPDH was approximately 41% bound. Bound ALD activity remaining in chemically demembranated Taenia coli was similar to that in intact tissue indicating a localization to the contractile apparatus. ALD was found to be specifically bound in the demembranated preparation. Chemical demembranation resulted in almost complete loss of all GAPDH activity indicating a localization of bound GAPDH to cellular membranes.

引用

页码：256 / 259

页数：4

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