Surface characteristics of teratoma cell populations and purification of teratoma adhesion factor

Specific subpopulations of 129/J mouse teratocarcinoma cells were separated in a large capacity reorienting gradient zonal rotor. The teratoma cells consistently separated into two major populations, small and large cells. Both cell populations were treated with two galactose-binding lectins: ricin agglutinin and peanut aggulutinin (RCA-I and PNA). Large cells were agglutinated by RCA-I. Although small cells bound both RCA-I and PNA, neither lectin caused the small cells to agglutinate. Thus, the large cells are more malignant-like with respect to lectin-mediated agglutination. Further progress has been made in the purification and characterization of teratoma adhesion factor (TAF) TAF was purified by affinity chromatography with RCA-II covalently bound to agarose. Factor activity was recoverable when the RCA-II-agarose column was eluted with a D-galactose gradient. SDS gel electrophoresis of purified TAF revealed four bands when stained with coomassie brilliant blue, a stain for protein. All of the protein bands stained PAS-positive {PAS is a stain for carbohydrate). The molecular weights of the proteins ranged from 27,000 to 145,000 daltons. These results add to the growing body of knowledge concerning teratoma adhesion factor.