Study on prolidase dificiency-in special reference to proline metabolism
Project/Area Number |
60570464
|
Research Category |
Grant-in-Aid for General Scientific Research (C)
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Allocation Type | Single-year Grants |
Research Field |
Dermatology
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Research Institution | Department of Dermatology, Kochi Medical School |
Principal Investigator |
ARATA Jiro Department of Dermatology, Kochi Medical School, Professor, 医学部, 教授 (70033082)
|
Project Period (FY) |
1985 – 1986
|
Project Status |
Completed (Fiscal Year 1986)
|
Budget Amount *help |
¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1986: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 1985: ¥1,100,000 (Direct Cost: ¥1,100,000)
|
Keywords | Prolidase deficiency / Substrate specificity / Heat stability / P-chloromercuribenzoic acid / Mn依存性 |
Research Abstract |
Prolidase and prolinase activities of cultured skin fibroblasts obtained from prolidase deficient sisters(symptom(+),symptom(-)) and two normal subjects were assayed. Results. I. prolidase activities against Gly-Pro, Leu-Pro, Val-Pro were decreased to about 3% of normal enzyme activities in both patients. However, prolidase activities against Met-Pro, Ala-Pro, Phe-Pro were notably present in these prolidase deficient patients. 2. With different concentrations of manganese (ImM, IOOmM, I M), prolidase activities against Gly-Pro of the normal subjects were highest with IOOmM manganese. However, the enzyme activities of the patients were highest with ImM. 3. The heat stability of prolidase against Met-Pro was assayed. The enzyme of the patients seemed to be slightly less stable than the controls. 4. The prolidase activies in both patients and normal subjects were suppressed with 0.05mM p-chloromercuribenzoic acids. However, preincubation of the enzyme solution with ImM manganese seemed to protect only the normal enzymes from being inhibited. 5. When the enzyme solution was preincubated with Gly-Pro, the prolidase activities against Met-Pro seemed to be inhibited only in the patients. Comment. In the prolidase deficiency, the enzyme activities against some substrates such as Gly-Pro were almost absent but the activities against other iminodipeptides with C-terminal proline were considerably present. We supposed that the results described above suggested that the enzyme proteins were not absent but were altered in prolidase deficiency. No remarkable changes of prolinase activities were found in spite of slightly higher activities in symptom(-) sister.
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Report
(1 results)
Research Products
(6 results)