title: Fatty acylation of murine Ia alpha, beta, and invariant chains.
abstract: 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.
authors.forename: S
authors.initials: S
authors.lastname: Simonis
authors.forename: S E
authors.initials: SE
authors.lastname: Cullen
mesh_terms: D000215:Acylation; D000818:Animals; D002855:Chromatography, Thin Layer; D005227:Fatty Acids / Q000378:metabolism*; D005802:Genes, MHC Class II; D008040:Genetic Linkage; D014644:Genetic Variation; D006238:Haploidy; D006649:Histocompatibility Antigens / Q000032:analysis / Q000235:genetics; D000949:Histocompatibility Antigens Class II / Q000032:analysis* / Q000235:genetics; D051379:Mice; D008810:Mice, Inbred C57BL; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D005227:Fatty Acids; D006649:Histocompatibility Antigens; D000949:Histocompatibility Antigens Class II; C024138:I-E-antigen; D010169:Palmitic Acids; D019308:Palmitic Acid