Transglutaminase activity in Yoshida ascites tumor cells.
Transglutaminase may be an important intracellular regulator of protein function through its ability to catalyze the calcium-dependent covalent linkage of primary amines to glutamine residues in peptide linkage with the generation of ammonia. This study provides further evidence that a major alteration in tumor cells is the marked decline in the expression of transglutaminase activity. This may alter its known protein cross-linking activity and favor lack of differentiation and proliferation.
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D007700:Kinetics; D008297:Male; D011700:Putrescine / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012517:Sarcoma, Yoshida / Q000201:enzymology*; D011503:Transglutaminases
D000217:Acyltransferases; D011503:Transglutaminases; D011700:Putrescine