小鼠单克隆亚基特异性抗体与酿酒酵母磷酸果糖激酶-1的相互作用。

Interaction of murine monoclonal subunit-specific antibodies with phosphofructokinase-1 from Saccharomyces cerevisiae.

作者信息

Kopperschläger G, Kriegel T, Birkenmeier G

机构信息

Institute of Biochemistry, Medical Faculty, University of Leipzig, Germany.

出版信息

FEBS Lett. 1995 Apr 17;363(1-2):17-21. doi: 10.1016/0014-5793(95)00269-f.

DOI:10.1016/0014-5793(95)00269-f

PMID:7729541

Abstract

Murine monoclonal subunit-specific antibodies against heterooctameric phosphofructokinase-1 from Saccharomyces cerevisiae exhibiting no cross-reactivity were purified and characterized regarding complex formation with the native enzyme, immunological reactivity to the SDS-denatured subunits originating from native and proteolytically truncated phosphofructokinase, and protection against proteolytic degradation. Strong complex formation was found with one alpha-specific antibody. Western blotting employing different enzyme forms allowed to localize epitope sites of the alpha-polypeptide chain. Monoclonal antibodies protect phosphofructokinase-1 against chymotryptic degradation.

摘要

针对酿酒酵母异源八聚体磷酸果糖激酶-1的无交叉反应性的鼠单克隆亚基特异性抗体被纯化，并对其与天然酶形成复合物、对源自天然和蛋白酶解截短的磷酸果糖激酶的SDS变性亚基的免疫反应性以及抗蛋白酶解降解能力进行了表征。发现一种α特异性抗体能形成强复合物。采用不同酶形式的蛋白质免疫印迹法可定位α多肽链的表位位点。单克隆抗体可保护磷酸果糖激酶-1免受胰凝乳蛋白酶降解。