Structural Requirements of Specific Substrates for Guinea Pig Liver Transglutaminase.
نویسندگان
چکیده
A &*-activated enzyme derived from the soluble fraction of guinea pig liver, and designated transglutaminase by Waelsch et al. (2-4) catalyzes the incorporation of a number of primary amines into certain proteins and polypeptides. There is evidence that this reaction proceeds via the replacement of amide groups of glutamine residues only (4, 5). Transglutaminase also catalyzes the release of ammonia from proteins in the absence of added amines (6). It has been suggested that this ammonia originates through hydrolytic cleavage of amide groups of certain protein-bound glutamine residues and that the same glutamine residues are involved in both the replacement. (a) and the hydrolysis (b) reactions (4, 6). These reactions may be formulated as follows.
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 240 شماره
صفحات -
تاریخ انتشار 1965