RESOLUTION OF THE MITOCHONDRIAL N,N'-DICYCLOHEXYLCARBODIIMIDE BINDING PROTEOLIPID FRACTION INTO 3 SIMILAR SIZED PROTEINS

被引：35

作者：

BLONDIN, GA ^{[1
]}

机构：

[1] INST ENZYME RES, MADISON, WI 53706 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 87卷 / 04期

关键词：

D O I：

10.1016/S0006-291X(79)80019-4

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：

Three chloroform-methanol soluble proteins were resolved by reverse phase high performance liquid chromatography of a [bovine] mitochondrial proteolipid fraction from Sephadex LH-60 containing predominantly hydrophobic proteins of < 10,000 daltons. While all 3 of the purified proteins comigrate during sodium dodecyl sulfate-urea gel electrophoresis, amino acid analyses of the purified components reveal major differences by which each can be easily distinguished. The 3 proteins occur in yields of 1.58, 0.28 and 0.21 nmol/mg protein, respectively, for proteins .alpha., .beta. and .gamma.. Only hydrophobic protein .alpha. is isolatable with N,N''-dicyclohexylcarbodiimide covalently bound, whereas hydrophobic proteins .beta. and .gamma. bind significant levels of ADP and Pi.

引用

页码：1087 / 1094

页数：8

共 21 条

[1]

BLONDIN G, UNPUBLISHED

[2]

BLONDIN GA, 1979, BIOPHYS J, V25, pA48

[3] MECHANISM OF MITOCHONDRIAL SWELLING .2. PSEUDOENERGIZED SWELLING IN PRESENCE OF ALKALI METAL SALTS [J].