抄録
N-Acetylglucosaminide β1→4 galactosyltransferase was chromatographically purified about 1, 700-fold from F9 embryonal carcinoma cells after solubilization with Triton X-100, using N-acetylglucosamine as the acceptor. As the last step of the purification, affinity chromatography was performed either on N-acetylglucosamine-Sepharose or on α-lactalbumin-Sepharose: in both cases, two protein bands with molecular weights of around 68, 000 and 59, 000 were detected by SDS-polyacrylamide gel electrophoresis of the purified preparations. The enzymological properties including behavior toward α-lactalbumin were very similar to those of the enzyme from other sources. The specificity of the enzyme was confirmed by determining the structure of the product; it was mostly Galβ1→4G1cNAc. β-Galactosidase-treated embryoglycan (poly-N-acetyllactosamine) and asialo-agalactofetuin could serve as acceptors with the purified enzyme. Thus, the embryonic enzyme, apparently involved in the synthesis of poly-N-acetyllactosamines, has properties similar in several respects to those of the β-galactosyltransferases so far studied.
