PURIFICATION AND CHARACTERIZATION OF A BASIC 23 KDA CYTOSOLIC PROTEIN FROM BOVINE BRAIN

被引：137

作者：

BERNIER, I

JOLLES, P

机构：

[1] UNIV PARIS 05, CNRS, ER 102, PROT LAB, F-75270 PARIS 06, FRANCE

[2] UNIV PARIS 05, INSERM, U116, F-75270 PARIS 06, FRANCE

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1984年 / 790卷 / 02期

关键词：

D O I：

10.1016/0167-4838(84)90221-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A soluble basic protein was purified from bovine brain. It is constituted by a single polypeptide chain with a MW of .apprx. 23 kDa [kilodalton] and an isoelectric point of .apprx. 8.6. The protein was further characterized by its amino-acid composition and by a 39 amino acid-long N-terminal sequence. Sequence homologies were demonstrated with some other cytosolic proteins. Ligand-binding assays revealed a significant ability of the 23-kDa protein for bromosulfophthalein. Immunochemical analysis using a rabbit anti 23-kDa brain protein antiserum demonstrated its simultaneous presence in bovine liver as well as in soluble extracts from different origins (mouse and rat brain; human platelets).

引用

页码：174 / 181

页数：8

共 26 条

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