Jul 13, 2005

Characterization of prolidase activity in erythrocytes from a patient with prolidase deficiency: comparison with prolidase I and II purified from normal human erythrocytes

Clinical Biochemistry
Gang LiuHiroyuki Kodama

Abstract

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. 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. 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. 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.

Mentioned in this Paper

Dialysis Solutions
Chloride Ion Level
Molecular Stereochemistry
Phosphate buffers
Enzymes, antithrombotic
Valine
2-Mercaptoethanol
SDS-PAGE
Amino Acids, I.V. solution additive
D-Serine

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