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: 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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Authors | Gang Liu, Kazuko Nakayama, Yasuhiro Sagara, Shiro Awata, Koichi Yamashita, Masanobu Manabe, Hiroyuki Kodama |
Journal | Clinical biochemistry
(Clin Biochem)
Vol. 38
Issue 7
Pg. 625-31
(Jul 2005)
ISSN: 0009-9120 [Print] United States |
PMID | 16009141
(Publication Type: Journal Article)
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Chemical References |
- Amino Acids
- Chlorides
- Dipeptides
- Manganese Compounds
- glycylproline
- Dipeptidases
- proline dipeptidase
- Valine
- manganese chloride
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Topics |
- Amino Acids
(pharmacology)
- Chlorides
(pharmacology)
- Dipeptidases
(blood, deficiency, isolation & purification)
- Dipeptides
(metabolism)
- Electrophoresis, Polyacrylamide Gel
- Erythrocytes
(enzymology)
- Humans
- Kinetics
- Manganese Compounds
(pharmacology)
- Stereoisomerism
- Valine
(pharmacology)
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