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dc.contributor.authorAgre, Peter
dc.contributor.authorde Vetten, Marcel P
dc.date.accessioned2010-05-10T15:04:09Z
dc.date.available2010-05-10T15:04:09Z
dc.date.issued1988-12-05
dc.identifier.citationJ Biol Chem 1988 Dec. 5, 1988: 18,193-18,196. http://www.jbc.org/content/263/34/18193.abstracten_US
dc.identifier.urihttp://jhir.library.jhu.edu/handle/1774.2/34102
dc.description.abstractThe erythrocyte Rh antigens contain an Mr = 32,000 integral protein which is thought to contribute in some way to the organization of surrounding phospholipid. To search for possible fatty acid acylation of the Rh polypeptide, intact human erythrocytes were incubated with [3H]palmitic acid prior to preparation of membranes and sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Several membrane proteins were labeled, but none corresponded to the glycophorins or membrane proteins 1-8. An Mr = 32,000 band was prominently labeled on Rh (D)-negative and -positive erythrocytes and could be precipitated from the latter with anti-D. No similar protein was labeled on membranes from Rhmod erythrocytes, a rare phenotype lacking Rh antigens. Labeling of the Rh polypeptide most likely represents palmitic acid acylation through thioester linkages. The 3H label was not extracted with chloroform/methanol, but was quantitatively eluted with hydroxylamine and co-chromatographed with palmitohydroxamate and free palmitate by thin layer chromatography. The fatty acid acylations occurred independent of protein synthesis and were completely reversed by chase with unlabeled palmitate. It is concluded that the Rh polypeptide is fatty acid-acylated, being a major substrate of an acylation-deacylation mechanism associated with the erythrocyte membrane.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen_US
dc.subjectRh polypeptidesen_US
dc.titleThe Rh polypeptide is a major fatty acid-acylated erythrocyte membrane proteinen_US
dc.typeArticleen_US


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