Subunit interactions of class I histocompatibility antigens.
Subunit interactions of class I histocompatibility antigens.
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I 类组织相容性抗原的亚基相互作用。
DOI:
10.1021/bi00341a039
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发表时间:
1985
期刊:
影响因子:
2.9
通讯作者:
Strominger,JL
中科院分区:
文献类型:
--
作者:
Parker,KC;Strominger,JL
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138 Received February 21, 1985 abstract: The kinetics of dissociation of iodinated d2-microglobulin (d2m) from the papain-solubilized class I histocompatibility antigen HLA-B7 have been investigated. In the presence of unlabeled/32m, most of the HLA dissociates according to a single rate constant, whereas in the absence of unlabeled/32m, the system approaches an equilibrium dependent upon the initial HLA concentration. When iodinated ß2 is incubated with unlabeled HLA-B7, the rate of incorporation of ß2 into the complex is much less dependent on the concentration than is expected for a simple association/dissociation system; instead, the systembehaves as if the “activity”(in a thermodynamic sense) of the HLA heavy-chain intermediate cannot surpass a critical concentration. The dissociation rate for each class I specificity is a function of temperature, ionic strength, pH, and the status of the heavy chain (papain solubilized vs. detergent solubilized). High temperature, high ionic strength, andextremes of pH promote dissociation. The intact molecule dissociates about 10 times more slowly than the papain-solubilized molecule. In contrast, the rate of dissociation of all pa-pain-solubilized class I antigens tested falls within the range of about a factor of 2. The presence of the carbohydrate has no effect on the rate of dissociation. The possibilitythat HLA class I antigen dissociation may occur in vivo within acidic internal vesicles is discussed.