N. C. Davis, E. L. Smith
1957
Citations
2
Influential Citations
82
Citations
Quality indicators
Journal
The Journal of biological chemistry
Abstract
In 1937, Bergmann and Fruton (3) recognized that glycyl-L-proline is hydrolyzed by an enzyme from intestinal mucosa which is distinct from previously known peptidaaes. Since that time, this enzyme, which was named prolidase, has been shown to be present in many animal tissues (4), the main features of its specificity have been delineated (2, 5, S), and it has been obtained in partially purified form from swine intestinal mucosa (7) and from equine erythrocytes (5). The specificity of prolidase is unique in so far as it is the only enzyme known which can catalyze the rapid hydrolysis of compounds in which the sensitive peptide bond involves the imino nitrogen of proline or hydroxyproline. Because there is only a small quantity of prolidase in animal tissues, extensive purification has not been reported previously. We now wish to describe methods by which prolidaae preparations may be obtained from swine kidney which are approximately 12,000 times more active than crude, aqueous extracts of this organ. Although only small amounts of this labile enzyme have been obtained, some of its properties have been determined and the characteristic features of its specificity, previously studied with cruder preparations from other sources, have been ascertained.