Rat pancreatic islet homogenates catalyze the incorporation of [2,5−3-H]histamine into endogenous proteins recovered in both the stacking gel and a Mr 84000 protein separated by polyacrylamide electrophoresis. The labelling of these proteins represents a Ca2+-dependent process inhibited by glycine methylester, but not sarcosine methylester, and enhanced after preincubation of the islets at a high concentration of D-glucose. Although transglutaminase activity is found in both soluble and particlate subcelluler fractions, the endogenous transglutaminase substrates were located mainly in paarticulate, possibly membrane-associated, material.
Transglutaminase-catalyzed incorporation of [2,5-3H]histamine into a Mr 84000 particulate protein in pancreatic islets
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Ramon Gomis, Angeles Casanovas, Willy J. Malaisse; Transglutaminase-catalyzed incorporation of [2,5-3H]histamine into a Mr 84000 particulate protein in pancreatic islets. Biosci Rep 1 February 1989; 9 (1): 55–61. doi: https://doi.org/10.1007/BF01117511
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