HUMAN ERYTHROCYTE-MEMBRANE PROTEIN-4.2 IS PALMITOYLATED

被引：17

作者：

DAS, AK ^{[1
]}

BHATTACHARYA, R ^{[1
]}

KUNDU, M ^{[1
]}

CHAKRABARTI, P ^{[1
]}

BASU, J ^{[1
]}

机构：

[1] BOSE INST, DEPT CHEM, Kolkata 700009, W BENGAL, INDIA

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 224卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1994.00575.x

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：

Protein 4.2 is a major protein of the human erythrocyte membrane. It has previously been shown to be N-myristoylated. After labeling of intact human erythrocytes with [H-3]palmitic acid, radioactivity was found to be associated with protein 4.2 by immunoprecipitation of peripheral membrane proteins extracted at pH 11 from ghosts with anti-(4.2) sera, followed by SDS/PAGE and fluorography. The fatty acid linked to protein 4.2 was identified as palmitic acid after hydrolysis of protein and thin-layer chromatography of the fatty acid extracted in the organic phase. Protein 4.2 could be depalmitoylated with hydroxylamine, suggesting a thioester linkage. Depalmitoylated protein 4.2 showed significantly decreased binding to protein-4.2-depleted membranes, compared to native protein 4.2.

引用

页码：575 / 580

页数：6

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