التفاصيل البيبلوغرافية
| العنوان: |
Isolation and Properties of Detergent-Solubilized HLA Antigens Obtained from Platelets. |
| المؤلفون: |
Trägardh, L., Klareskog, L., Curman, B., Rask, L., Peterson, P. A. |
| المصدر: |
Scandinavian Journal of Immunology; Apr1979, Vol. 9 Issue 4, p303-314, 12p |
| مصطلحات موضوعية: |
HLA histocompatibility antigens, BLOOD platelets, CYTOPLASM, LIPOSOMES, PHOSPHOLIPIDS, BILAYER lipid membranes, COLLOIDS |
| مستخلص: |
Deoxycholate-solubilized HLA antigens have been isolated from platelets and comprised a mixture of 43,000- and 39,000-dalton polypeptide 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 of the 39,000-dalton comcomponent are charged. The proteolytic split most 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-dalton components bind detergent in micellar form and can be incorporated into liposomes. The 33,000-dalton fragment has lost the ability to bind detergent micelles and is not incorporated into liposomes. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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