The presence of the pyrrolidonyl peptidase activity in many tissues of pig, cow, rabbit, guinea-pig, rat, mouse, pigeon, hen and carp has been demonstrated. It was also found in some human tissues and in plants. The enzyme from the pigeon liver was partially purified and some of its properties were studied. By means of gel filtration of the pigeon and rabbit liver homogenates two enzyme fractions were separated and their molecular weight was estimated. The enzyme activity was inhibited by some ions, by –SH-blocking reagents, by pyrrolidone carboxylic acid and polyvinylpyrrolidone. Its specifity seemed to be connected only with pyrrolidonecarboxylyl group, present in the substrate molecule.
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Szewczuk et al. (1970) studied this question.
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