Fatty acylation of murine Ia alpha, beta, and invariant chains.
Labeling of murine spleen cells with [3H]palmitate followed by analysis of immunoprecipitated Ia molecules indicated that Ia alpha- and beta-chains and their associated invariant chain contain covalently bound fatty acid. This modification is present in I-A and I-E molecules and has been found in all haplotypes examined. The 3H label was not dissociated from the glycoproteins by detergents or under the denaturing conditions of SDS-polyacrylamide gel electrophoresis. The fatty acid linked to Ii is released by treatment with neutral hydroxylamine, which indicates thioester linkage. The acylation of alpha- and beta-chains appears to involve attachment of palmitoyl groups via an ester linkage sensitive to alkaline hydrolysis. The radioactive species released from the isolated chains by treating with KOH/methanol co-migrated with palmitic acid and palmitic acid methyl ester on thin-layer chromatography.[1]References
- Fatty acylation of murine Ia alpha, beta, and invariant chains. Simonis, S., Cullen, S.E. J. Immunol. (1986) [Pubmed]
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