ISSN:
1365-3083
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Deoxycholate-solubilized HLA antigens have been isolated from plalelets and comprised a mixture of 43,000- and 39,000-dalton polypcptide chains associated with β2-microglobulin. Limited proteolysis experiments suggested that the 39,000-dalton chain is a fragment of the intact 43,000-dalton chain. Further proteolysis of the 39,000-dalton fragment yields a 33,000-dalton component. The 39,000-dalton molecule is more acidic than both the 43,000- and the 33,000-dalton chains. Differences in the amino acid compositions of the 43,000- and 39,000-dalton species demonstrate that the peptide(s) released on generation ofthe 39,000-dalton com-coniponent are charged. The proieolytic split mosl probably occurs in the COOH-terminal end which, owing to its content of charged amino acids, most probably is not integrated into the hydrocarbon matrix of the membrane. The 39,000- and 43,000-dall on components bind detergent in micellar form and can be incorporated into liposonies. The 33,000-dalton fragment has lost the ability to bind detergent micelles and is not incorporated into liposomes
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-3083.1979.tb03168.x
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