Abstract: | The cell surface glycoproteins of hamster NIL cells, labeled with galactose oxidase and NaB3H4, were selectively solubilized by sequential extraction with Tris buffer containing 1) sucrose-ATP-EDTA, 2) zwitterionic detergent (Empigen BB), and 3) 8 M urea. The previously reported “galactoprotein b” and “galactoprotein a” ( or LETS) were isolated by affinity chromatography on insoluble Ricinus communis lectin colums (RCA column) from extracts 2) and 3), respectively. The affinity-purified contained an actin-like protein, whereas the other affinity-purified galactoproteins did not contain the actin-like protein. The isolated was heterogeneous, and an additional glycoprotein, specific for NILpy cells was copurified on RCA-column with . |