Open AccessComparative Studies of Mouse (H‐2) and Human (HL‐A) Histocompatibility Antigens
Author(s) -
Hess Maxime,
Smith William
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03434.x
Subject(s) - sephadex , antigen , locus (genetics) , histocompatibility , electrophoresis , chemistry , major histocompatibility complex , microbiology and biotechnology , urea , biochemistry , biology , gene , human leukocyte antigen , enzyme , genetics
A purification procedure applied to H‐2 antigens (controlled by the H‐2 locus) was used for the characterization of HL‐A substances (HL‐A2 and HL‐A7) (controlled by the HL‐A locus) solubilized from lymphoid cell membranes by delipidation. Upon Sephadex chromatography the serologically active material had an apparent M r of 32000, and displayed, in relation to H‐2 antigens, a faster electrophoretic mobility and higher p I values. One sulfhydryl group and one (intrachain) disulfide bond were present in partially purified HL‐A preparations. Reduction and aminoethylation in 4 M urea did not influence the electrophoretic migration of HL‐A active substances, suggesting that, as already demonstrated for H‐2 alloantigens, in HL‐A molecules the genetic determinants are present on single polypeptide chains. Highly purified HL‐A alloantigens, like H‐2 substances, revealed a high degree of microheterogeneity. These findings further support the concept of the genetic and structural homology of the main histocompatibility systems in mouse and man.