A NEW HIGH-YIELD PROCEDURE FOR THE PURIFICATION OF THE NONSPECIFIC PHOSPHOLIPID TRANSFER PROTEIN FROM RAT-LIVER

被引：98

作者：

POORTHUIS, BJHM ^{[1
]}

GLATZ, JFC ^{[1
]}

AKEROYD, R ^{[1
]}

WIRTZ, KWA ^{[1
]}

机构：

[1] STATE UNIV UTRECHT, BIOCHEM LAB, TRANSITORIUM 3, 3508 TB UTRECHT, NETHERLANDS

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1981年 / 665卷 / 02期

关键词：

D O I：

10.1016/0005-2760(81)90010-2

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：

Rat liver contains a non-specific phospholipid transfer protein that transfers phosphatidylethanolamine, phosphatidylcholine, phosphatidylinositol and sphingomyelin as well as cholesterol between membranes. A new high-yield procedure for the purification of this protein, which includes fractionation on DEAE-cellulose, Sephadex G-50 and hydroxyapatite is described. Starting from a pH 5.1 supernatant, a homogeneous protein was obtained after a 1,540-fold purification at a yield of 50%. The protein has a MW of 14,800 as estimated by electrophoresis on polyacrylamide gels in the presence of sodium dodecyl sulfate. It has a blocked N-terminal amino acid and a tryptophanyl fluorescence emission maximum at 335 nm. Its amino acid composition was determined and compared to data published by others on similar proteins.

引用

页码：256 / 261

页数：6

共 18 条

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