Transglutaminase-catalyzed cross-linking through diamines and polyamines.
Transglutaminases were found to catalyze the formation of cross-links between peptide chains by means of a transfer reaction between the carboxamide group of a glutamine residue in each chain and both primary amino groups of a diamine or a polyamine. Production of this heretofore undescribed linkage by guinea pig liver transglutaminase was demonstrated by the use of high performance liquid chromatography in a model system using glutamine peptide derivatives and a variety of diamines and polyamines. Evidence for intermolecular cross-linking through polyamines with both the liver enzyme and thrombin-activated human plasma blood coagulation factor XIII was obtained by the use of a guanidinated derivative of beta-casein.
D000818:Animals; D003959:Diamines; D006168:Guinea Pigs; D006834:Hydrazines; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D011073:Polyamines; D005723:gamma-Glutamyltransferase / Q000378:metabolism*
D003959:Diamines; D006834:Hydrazines; D011073:Polyamines; D005723:gamma-Glutamyltransferase