UDP-N-acetylglucosamine 2'-epimerase of rat hepatoma and its comparison with the enzyme of rat liver.
UDP-N-acetylglucosamine 2'-epimerase was partially purified from Yoshida sarcoma, a strain of rat ascites hepatoma, by (NH4)2SO4 precipitation followed by TEAE-cellulose chromatography. The purified enzyme was inhibited by CMP-N-acetylneuraminic acid to similar extent to partially purified rat liver 2'-epimerase. Although the two enzymes were also similar in Km for UDP-N-acetylglucosamine, they were differentiated by chromatography on TEAE-cellulose, DEAE-Sephadex and hydroxyapatite, tumor enzyme being less tightly bound to these columns than liver enzyme. Similar chromatographic difference was also noted between 2'-epimerases of mouse liver and mouse Ehrlich asites carcinoma.
D000818:Animals; D002238:Carbohydrate Epimerases / Q000302:isolation & purification*; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology; D008099:Liver / Q000201:enzymology*; D008114:Liver Neoplasms, Experimental / Q000201:enzymology*; D008297:Male; D051379:Mice; D051381:Rats; D012517:Sarcoma, Yoshida / Q000201:enzymology*
D002238:Carbohydrate Epimerases