Purification and Calcium Dependence of Transglutaminases from Sheep Hair Follicles
Copyright policy )Purification and Calcium Dependence of Transglutaminases from Sheep Hair Follicles
To study the calcium sensitivity of sheep hair follicle transglutaminase, which was reportedly calcium-independent [H. W. Harding and G.E. Rogers, Biochemistry, 11, 2858-2863 (1972)], the enzyme was purified from a homogenate of merino sheep hair follicles and its calcium dependence was examined. As a result of purification, two types of transglutaminases (DEAE-unabsorbed and absorbed transglutaminase, DU-TG and DA-TG, respectively) were obtained. The molecular mass of DU-TG was 77 and 82 kDa by SDS-PAGE and gel filtration, respectively, while that of DA-TG was 40 and 80 kDa. Each enzyme was obviously calcium dependent and contained (a) cysteine residue(s) in the active site, like other known mammalian transglutaminases. Maximum activation of DU-TG and DA-TG was observed at 1 and 0.1 mM CaCl2, respectively.
- Ajinomoto United States
Male, Sheep, Transglutaminases, Temperature, Caseins, Dipeptides, Hydrogen-Ion Concentration, Molecular Weight, Cross-Linking Reagents, Animals, Insulin, Calcium, Enzyme Inhibitors, Hair Follicle
Male, Sheep, Transglutaminases, Temperature, Caseins, Dipeptides, Hydrogen-Ion Concentration, Molecular Weight, Cross-Linking Reagents, Animals, Insulin, Calcium, Enzyme Inhibitors, Hair Follicle
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