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- W2507265958 abstract "Detergent and papain solubilized murine histocompatibility (H-2) antigens have been compared by gel exclusion chromatography, ultracentrifugation, sodium dode- cyl sulfate-polyacrylamide gel electrophoresis, and amino- acid sequence analysis. From these data, we propose a mo- lecular model for the H-2 antigens that includes the size and arrangement of the subunits on the cell surface and in solu- tion, and we provide evidence for the orientation of these molecules on the cell surface. Detergent solubilized H-2 anti- gens (molecular weight 116,000) consist of two disulfide- linked heavy chains (46,000 daltons) and two noncovalently associated light chains (12,000 daltons). Alkylation with iodo- acetamide prior to extraction prevented the formation of a disulfide linkage between the two heavy chains. A water-sol- uble 51,000-dalton molecule (Fs) consisting of a 39,000-dalton fragment (FH) of the heavy chain and one intact light chain was obtained by papain digestion of cells or detergent ex- tracts. Therefore, the disulfide linkage between the heavy chains is located in the remaining membrane-associated por- tion (Fm). Amino-acid sequence analysis of the FH fragment of H-2Kb by radiochemical techniques showed that it is iden- tical to the detergent solubilized H-2Kb heavy chain in eight positions for the three amino acids tested. These data indi- cate that the fragment FH derives from the amino-terminus of the heavy chain and suggest that it projects outward from the cell surface, while the carboxyl-terminal region is associ- ated with the plasma membrane. The described amino-termi- nal sequence data have been found constant in H-2Kb, H- 2Kd, H-2Kk, H-2Db, and H-2Dd gene products. These data support the hypothesis that the K and D products of the major histocompatibility antigen complex have evolved by gene duplication. The importance of histocompatibility antigens in the rejec- tion of allografts has been established, but the molecular structure and biological function of these cell-surface glyco- proteins are largely unknown. Recent studies support the no- tion that these molecules function in the discrimination of" @default.
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- W2507265958 date "2016-01-01" @default.
- W2507265958 modified "2023-09-23" @default.
- W2507265958 title "Subunit structure, cell surface oric sequences of murine histocompatib (detergent and papain solubilized H-2 antigens/molecular weigh" @default.
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