豚鼠结肠带中两种糖酵解酶的定位

Localization of two glycolytic enzymes in guinea-pig taenia coli.

作者信息

Hardin C D, Paul R J

机构信息

Department of Physiology and Biophysics, University of Cincinnati, OH.

出版信息

Biochim Biophys Acta. 1992 Apr 7;1134(3):256-9. doi: 10.1016/0167-4889(92)90184-d.

DOI:10.1016/0167-4889(92)90184-d

PMID:1558849

Abstract

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.

摘要

在完整的结肠带绦虫中测量了3-磷酸甘油醛脱氢酶（GAPDH）和1,6-二磷酸果糖醛缩酶（ALD）的结合部分。ALD约60%被结合，GAPDH约41%被结合。化学去膜的结肠带绦虫中剩余的结合型ALD活性与完整组织中的相似，表明其定位于收缩装置。发现ALD在去膜制剂中特异性结合。化学去膜导致所有GAPDH活性几乎完全丧失，表明结合型GAPDH定位于细胞膜。