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Isolation and Properties of Detergent‐Solubilized HLA Antigens Obtained from Platelets
Author(s) -
TRÄGÅRDH L.,
KLARESKOG L.,
CURMAN B.,
RASK L.,
PETERSON P. A.
Publication year - 1979
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1979.tb03168.x
Subject(s) - proteolysis , chemistry , biochemistry , peptide , micelle , solubilization , membrane , amino acid , platelet , liposome , antigen , chromatography , enzyme , biology , organic chemistry , aqueous solution , immunology , genetics
Deoxycholate‐solubilized HLA antigens have been isolated from plalelets and comprised a mixture of 43,000‐ and 39,000‐dalton polypcptide chains associated with β 2 ‐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