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Title: Fatty acylation of murine Ia. cap alpha. ,. beta. , and invariant chains

Journal Article · · J. Immunol.; (United States)
OSTI ID:6937186

Labeling of murine spleen cells with (/sup 3/H)palmitate followed by analysis of immunoprecipitated Ia molecules indicated that Ia ..cap 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 /sup 3/H-label was not dissociated from the glycoproteins by detergents or under the denaturing conditions of SDS-polyacrylamide gel electrophoresis. The fatty acid linked to I/sub i/ is released by treatment with neutral hydroxylamine, which indicates thioester linkage. The acylation of ..cap 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.

Research Organization:
Washington Univ. School of Medicine, St. Louis, MO
OSTI ID:
6937186
Journal Information:
J. Immunol.; (United States), Vol. 136:8
Country of Publication:
United States
Language:
English