Properties of Purified Papain-solubilized Rat AgB Antigens and Reactivity of a Xenoantiserum against the Isolated Antigens

Publisher Website
Google Scholar
Abstract
Rat AgB transplantation antigens were isolated after papain digestion of spleens from the inbred strain Hooded Lister. Both subunits of the AgB antigens were present in the purified material. Some physical characteristics of the antigens were determined. An antiserum, raised in a rabbit, against the purified material reacted exclusively with AgB antigens on splenocytes but detected novel structures on adult and embryonic fibroblasts. These structures, antigenically related to AgB antigens, were not detected on plasmacytoma or hepatoma cells, nor did they display any antigenic similarity with rat .beta.2-microglobulin. Radioimmunoassays specific for the AgB antigen H chain and for .beta.2-microblogulin, respectively, were used to estimate the contents of these antigens in several tissues. Spleen and thymus exhibit the largest density, while brain is almost devoid of these antigens.