1990 Fiscal Year Final Research Report Summary
The Cause of Prolidase Deficiency and Medical Treatment in Patients with Prolidase Deficiency
| Project/Area Number |
01570162
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Kochi Medical School |
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Principal Investigator |
KODAMA Hiroyuki Kochi Medical School, Chemistry, Prof., 医学部, 教授 (70032886)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAMURA Hiroyo Kochi Medical School, Chemistry, Researcher, 医学部, 教務員 (60217891)
OHNO Takashi Okayama Univ. Medical School, Assist. Prof., 医学部, 助手 (80203884)
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| Project Period (FY) |
1989 – 1990
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| Keywords | prolidase deficiency / chronic ulcerative dermatities |
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| Research Abstract |
Two forms of prolidase could be separated from erythrocytes of normal subjects and mother of patients with prolidase deficiency using TSK DEAE-5PE Chromtatography.
Only one form of prolidase was separated from erythrocytes of patients of with prolidase dificiency.
Each peak (I and II) of prolidase differed in their response to Mn^<2+>, substrate specificity and heat stability. Prolidase activity in erythrocytes form patients with prolicdase deficiency showed complete lack of normal prolidase, whereas peak II had normal activity against all the substrated tested. The various properties between patients' prolidase and peak II of normal prolidase were very similar.
Prolidase I (EC 3.4.13.9) have been purified to homogeneity from the erythrocytes of normal human and patient's mother.
Prolidase I from normal human and patient's mother have as molecular weight of about 112,000 and are composed of two subunits identical in molecular weight of 56,000.
The Km values from gly-pro of normal and patient mother's prolidase I were 2.90 and 2.88 mM, but the Vmax values for gly-pro of mother's enzyme was reduced about 30% compared to that of normal enzymes (mother : 6.02 units/mg protein).
Isonic points of those enzymes by chromatofocusing were pH 4.6-4.7.
Prolidase II from erythrocytes of normal human, and patient's mother, and prolidase from patient's erythrocytes have also been purified highly. Prolidase II from normal human, patient's mother and patient's prolidase have a molecular weight of about 185,000, and are composed of two subunits identical in molecular weight of 95,000. The Km and Vmax balues for various substrates of these enzymes are almost same. The chronic ulcerative dermatities of a patient with prolidase deficiency cured temporally by administration of glycine and proline.
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