The sensitivity of tissue transglutaminase to activation by Ca2+ and other cellular factors was investigated using the enzyme purified from rat liver. The inclusion of Mg2+ in the assay system appeared to reduce the Ca2+-requirement of the enzyme when native N,N′-dimethylcasein was used as the protein acceptor substrate. However, when this protein was dephosphorylated, the Ca2+-requirement was unaffected by Mg2+. In addition, using this modified assay, a Km for Ca2+ was calculated to be in the range of 3–4 μM, at least an order of magnitude lower than that obtained with native acceptor substrate. Membrane phospholipids, 1,2-diolein and calmodufin were found not to affect the activation oftransglutaminase by Ca2+. The sensitivity of transglutaminase to Ca2+ which we have now demonstrated suggests that this enzyme may directly act as a receptor protein for Ca2+ during stimulusresponse coupling mediated by this cation.
Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein
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D. Hand, P. J. Bungay, B. M. Elliott, M. Griffin; Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein. Biosci Rep 1 December 1985; 5 (12): 1079–1086. doi: https://doi.org/10.1007/BF01119629
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