期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1972
卷号：69
期号：1
页码：223-227
DOI：10.1073/pnas.69.1.223
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Histocompatibility antigens solubilized from cell-membrane fragments of BALB/c mouse spleen and liver, by Triton X-100 and butyl alcohol, were subjected to digestion by proteolytic enzymes in an effort to obtain smaller molecular species that retained antigenic activity. Digestion with both trypsin and papain yielded two antigens of smaller molecular weights that retained the specificity of BALB/c histocompatibility antigen, as determined by the inhibition of allogeneic antibodies, agglutination of BALB/c erythrocytes, adsorption-hemagglutination versus the soluble histocompatibility antigen, and suppression of the ability of BALB/c spleen cells to produce hemolytic plaques to sheep erythrocytes. The two active products of trypsin digestion were, respectively, excluded by Sephadex G-50 but not by G-75, and excluded by G-25 but not by G-50. Papain digestion yielded one active antigen that was excluded by G-25 but not by G-50, and a smaller antigen that was excluded by G-10 but not by G-15 and, as determined by gel filtration, has a molecular weight slightly lower than vitamin B12.
