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  • Title: Characterization of prolidase activity in erythrocytes from a patient with prolidase deficiency: comparison with prolidase I and II purified from normal human erythrocytes.
    Author: Liu G, Nakayama K, Sagara Y, Awata S, Yamashita K, Manabe M, Kodama H.
    Journal: Clin Biochem; 2005 Jul; 38(7):625-31. PubMed ID: 16009141.
    Abstract:
    OBJECTIVES: The purpose of this study was to investigate the effect of various amino acids and their metabolites on the activities of prolidase I and II from human erythrocytes compared to those in a patient with prolidase deficiency. DESIGN AND METHODS: Prolidase I and II from human erythrocytes were purified by using column chromatography. Prolidase activity against various iminodipeptides was determined by spectrophotometry using Chinard's method. RESULTS: The activities of prolidase I and II against glycylproline and methionylproline were enhanced by glycine, L- and D-isoforms of alanine and serine and D-isoforms of valine, leucine and isoleucine. L-isoforms of branched amino acids inhibited the activity of prolidase I. On the other hand, the activity of prolidase II was enhanced by all of these L-branched amino acids. The patient's prolidase activity was also enhanced by all the L- and D-branched amino acids. CONCLUSION: The activities of prolidase I and II against various iminodipeptides were prominently enhanced by glycine, but the effect of L-valine differed between the two enzymes. Enzymatic properties of the patient's prolidase were essentially the same as those of prolidase II.
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