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- W2065682073 abstract "Transglutaminase, a Ca++-activated enzyme first described by Waelsch and co-workers, catalyzes the replacement of the amide groups of protein and peptide bound glutamine residues by primary amines (1, 2). The replaced amide appears as ammononia. Folk and Cole have recently presented a detailed study of this reaction with particular reference to the specificity of transglutaminase (3). Transglutaminase activity has been observed in various animal tissues such as liver, heart, kidney, spleen, lung and pancreas (1, 2, 4). We have confirmed the presence of this enzyme in rabbit and rat heart and further demonstrated transglutaminase activity in other muscle tissues such as the uterus and the skeletal muscle of the rat (5). Since this enzyme is present in muscle tissues the amine acceptor properties of some of the muscle proteins were studied. In this communication we report the transglutaminase catalyzed incorporation of putrescine into actin and tropomyosin. Experiments are also presented which indicate that this enzyme can utilize these muscle proteins not only as amine acceptors but also as amine donors, thereby, connecting these two proteins together with covalent bonds." @default.
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- W2065682073 date "1966-01-01" @default.
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- W2065682073 title "Enzymatic labelling of actin and tropomyosin with 14C-labelied putrescine" @default.
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- W2065682073 doi "https://doi.org/10.1016/0006-291x(66)90606-1" @default.
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