[成年牛小脑蛋白质和糖蛋白的分析。II. 伴刀豆球蛋白A琼脂糖凝胶层析定量分离]

[Analysis of proteins and glycoproteins from adult bovine cerebellum. II. Quantitative separation by Con A Sepharose chromatography].

作者信息

Corsi P, Gennarini G, Ruccia D, Vitiello F, Di Benedetta C

出版信息

Boll Soc Ital Biol Sper. 1980 May 30;56(10):1071-7.

Abstract

Soluble and insoluble glycoproteins from adult bovine cerebellum have been separated by affinity chromatography on ConA-Sepharose and analyzed by polyacrylamide gel electrophoresis I2% in presence of SDS. Soluble fraction represents 26% of total proteins. Within soluble and insoluble fractions 4.5% of proteins binds to ConA. Electropherograms of the soluble and insoluble fractions as well as of the proteins not absorbed on ConA-Sepharose, display a very complex pattern. Soluble fractions present many sharp bands in the region of molecular weight above 100 k. Heterogeneity is lesser in ConA-binding proteins. The contamination by Concanavalin A is considered. At present no definite conclusions can be drawn regarding the similarities existing between s.c. soluble and membrane-bound cerebral glycoproteins.

摘要

来自成年牛小脑的可溶性和不溶性糖蛋白已通过伴刀豆球蛋白A-琼脂糖亲和层析进行分离，并在十二烷基硫酸钠存在的情况下通过12%聚丙烯酰胺凝胶电泳进行分析。可溶性部分占总蛋白的26%。在可溶性和不溶性部分中，4.5%的蛋白质与伴刀豆球蛋白A结合。可溶性和不溶性部分以及未被伴刀豆球蛋白A-琼脂糖吸附的蛋白质的电泳图谱显示出非常复杂的模式。可溶性部分在分子量高于100k的区域呈现许多清晰的条带。伴刀豆球蛋白A结合蛋白中的异质性较小。考虑到伴刀豆球蛋白A的污染情况。目前，关于可溶性和膜结合脑糖蛋白之间存在的相似性，无法得出明确结论。

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