Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not
glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the
presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross
linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptides. Liver transglutaminase is a nonzymogenic
enzyme. https://www.creative-enzymes.com/product/Transglutaminase-From-Guinea-Pig-Liver-Recombinant_3440.html