伴刀豆球蛋白A与小牛脑突触小泡的结合。

Binding of concanavalin A to calf brain synaptic vesicles.

作者信息

March P E, Thornton E R

出版信息

Biochem Biophys Res Commun. 1983 Feb 10;110(3):804-10. doi: 10.1016/0006-291x(83)91033-1.

Abstract

Concanavalin A was employed as a tool to investigate the organization of synaptic vesicle glycoproteins. The lectin was incubated in the presence of both intact and Triton X-100 treated calf brain synaptic vesicles. Electrophoresis of treated membranes clearly demonstrated that the majority of Concanavalin A binding sites was not exposed in intact synaptic vesicles. The vesicles were isolated by the procedure of DeLorenzo and Freedman (DeLorenzo, R. J., and Freedman, S. D. (1978) Biochem. Biophys. Res. Commun. 80, 183-192). However, an extra centrifugation step at 55,000 g was required to obtain plain vesicles nearly free from coated vesicles and membrane fragments.

摘要

刀豆球蛋白A被用作研究突触小泡糖蛋白组织的工具。将该凝集素在完整的和经Triton X-100处理的小牛脑突触小泡存在的情况下进行孵育。对处理过的膜进行电泳清楚地表明，大多数刀豆球蛋白A结合位点在完整的突触小泡中并未暴露。突触小泡通过DeLorenzo和Freedman的方法分离（DeLorenzo, R. J., and Freedman, S. D. (1978) Biochem. Biophys. Res. Commun. 80, 183 - 192）。然而，需要在55,000 g下进行额外的离心步骤以获得几乎不含被膜小泡和膜碎片的纯净小泡。