PURIFICATION AND CHARACTERIZATION OF TETRAHYMENA PROFILIN

被引：8

作者：

EDAMATSU, M ^{[1
]}

HIRONO, M ^{[1
]}

WATANABE, Y ^{[1
]}

机构：

[1] UNIV TSUKUBA,INST BIOL SCI,TSUKUBA,IBARAKI 305,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 170卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)92184-2

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：

We subjected Tetrahymena cell extract to a poly(L-proline) affinity column for isolating profilin and obtained a protein of 12.8 kDa. Purified 12.8 kDa protein dose-dependently inhibited the polymerization of Tetrahymena actin more strongly than that of rabbit skeletal muscle actin. Because the 12.8 kDa protein fulfills properties common to profilins, the protein is considered to be Tetrahymena profilin. The present paper is the first report of the isolation of an actin-binding protein from Tetrahymena. © 1990.

引用

页码：957 / 962

页数：6

共 18 条

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