Alteration in glycosidases from well-differentiated colorectal adenocarcinoma of rat.
The activities of six glycosidases in a rat colorectal adenocarcinoma were measured and compared with those of normal colonic mucosa. The specific activities of beta-galactosidase (EC 3.2.1.23) and beta-glucuronidase (EC 3.2.1.31) in the adenocarcinoma were similar to those of the corresponding ones in the normal mucosa, whereas those of beta-N-acetylglucosaminidase (EC 3.2.1.30), alpha-L-fucosidase (EC 3.2.1.51), alpha-galactosidase (EC 3.2.1.22) and beta-glucosidase (EC 3.2.1.21) were reduced in the former as compared with those in the latter. In the case of alpha-L-fucosidase, two forms were newly detected in the tumor. The relative abundance of three forms of beta-N-acetylglucosaminidase was quite different between the adenocarcinoma and the normal mucosa, and the level of the intermediate form in the tumor was markedly reduced. However, thermostability and Km values of two forms A and B in the tumor were not different from those of the corresponding ones in the normal tissue.
D000230:Adenocarcinoma / Q000201:enzymology*; D000818:Animals; D003106:Colon / Q000201:enzymology; D003110:Colonic Neoplasms / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000097:blood / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000201:enzymology; D007700:Kinetics; D051381:Rats; D011912:Rats, Inbred ACI; D012004:Rectal Neoplasms / Q000201:enzymology*
D006026:Glycoside Hydrolases