A Reversible, Calcium-dependent, Copper-catalyzed Inactivation of Guinea Pig Liver Transglutaminase

Structural properties of guinea pig liver transglutaminase.

Evidence is presented that transglutaminase is composed of a single polypeptide chain of molecular weight 80,000 to 90,000. (a) Polyacrylamide gel electrophoresis in the presence of dodecyl sulfate and mercaptoethanol gave a single band with a mobility corresponding to a molecular weight of approximately 85,000. (b) Gel filtration in guanidine HCl of the 14C-carbamidomethyl carboxymethylated en...

Mechanism of the inactivation of guinea pig liver transglutaminase by 5,5'-dithiobis-(2-nitrobenzoic acid).

Reaction of 5,5’-dithiobis(24trobenzoic acid) (DTNB) with transglutaminase in the absence of calcium ion results in losses in the transferase and hydrolysis activities of the enzyme toward the substrate, benzyloxycarbonyl-L-glutaminylglycine (Z-L-glutaminylglycine). These activities are reduced 70 to 100% by reaction with 1 to 1.5 eq of DTNB. The calcium-dependent esterase activity of transglut...

Specific fluorescent labeling of chicken myofibril Z-line proteins catalyzed by guinea pig liver transglutaminase

Guinea pig liver transglutaminase has been found to catalyze the covalent incorporation of dansylcadaverine into chicken skeletal muscle myofibril proteins. Epifluorescence microscopy reveals that the incorporated dansylcadaverine is specifically localized at or near the myofibril Z line. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) indicates that actin constitutes a major fraction of the ...

Structural Requirements of Specific Substrates for Guinea Pig Liver Transglutaminase.

A &*-activated enzyme derived from the soluble fraction of guinea pig liver, and designated transglutaminase by Waelsch et al. (2-4) catalyzes the incorporation of a number of primary amines into certain proteins and polypeptides. There is evidence that this reaction proceeds via the replacement of amide groups of glutamine residues only (4, 5). Transglutaminase also catalyzes the release of am...

Identification of a functional cysteine essential for the activity of guinea pig liver transglutaminase.