通过亲和色谱和离子交换色谱联用从蓖麻中纯化凝集素并对分离出的蛋白质进行表征。

Purification and lectins from Ricinus communis by combination of affinity and ion-exchange chromatography and characterization of the isolated proteins.

作者信息

Genaud L, Guillot J, Bétail G, Coulet M

出版信息

J Immunol Methods. 1982 Mar 26;49(3):323-32. doi: 10.1016/0022-1759(82)90132-6.

Abstract

Lectins in the seeds of Ricinus communis L. were separated by affinity chromatography using stromata, and 3 fractions obtained by ion-exchange chromatography. Polyacrylamide-gel electrophoresis showed that 2 fractions were homogeneous and that 1 fraction gave 2 bands. Immunoelectrophoresis with rabbit antisera and polyacrylamide-gel isoelectric focusing showed that the 3 fractions were separate and distinct entities consisting of many proteins with isoelectric points near the isoelectric point of the main protein. The molecular weights of the separated proteins and their subunits were studied by SDS polyacrylamide-gel electrophoresis.

摘要

用子座通过亲和层析法分离蓖麻种子中的凝集素，并通过离子交换层析法得到3个组分。聚丙烯酰胺凝胶电泳表明，其中2个组分是均一的，另1个组分出现2条带。用兔抗血清进行免疫电泳和聚丙烯酰胺凝胶等电聚焦表明，这3个组分是分离的、不同的实体，由许多等电点接近主要蛋白质等电点的蛋白质组成。通过SDS聚丙烯酰胺凝胶电泳研究了分离出的蛋白质及其亚基的分子量。