Human erythrocyte membrane protein 4.2 is palmitoylated

Das, Amit K. ; Bhattacharya, Raja ; Kundu, Manikuntala ; Chakrabarti, Parul ; Basu, Joyoti (1994) Human erythrocyte membrane protein 4.2 is palmitoylated European Journal of Biochemistry, 224 (2). pp. 575-580. ISSN 0014-2956

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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1432-...

Related URL: http://dx.doi.org/10.1111/j.1432-1033.1994.00575.x

Abstract

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 [3H]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.

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Deposited On:05 Oct 2010 12:12
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