Project/Area Number |
07660115
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
応用微生物学・応用生物化学
|
Research Institution | Kumamoto University |
Principal Investigator |
UYEDA Masaru Kumamoto University, Pharmaceutical Sciences, Professor., 薬学部, 教授 (80038231)
|
Co-Investigator(Kenkyū-buntansha) |
SUZUKI Keitarou Kumamoto University, Pharmaceutical Sciences, Assistant professor., 薬学部, 助教授 (10154535)
|
Project Period (FY) |
1995 – 1996
|
Project Status |
Completed (Fiscal Year 1996)
|
Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1996: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1995: ¥1,600,000 (Direct Cost: ¥1,600,000)
|
Keywords | phospholipase / S-Hemolysin / Streptomyces sp. / inhibitor / S-PLI / SHI / sphingomyelinase / glycoprotein / Sphingomyelinase |
Research Abstract |
A new cytolytic toxin, designated as S-Hemolysin, was found in the culture filtrate of Streptomyces sp.strain No.A-6288. This enzyme was shown to be different from the known bacterial phospholipase C.A molecular weight of S-Hemolysin was estimated to be 10,000 and it is a glycoprotein that is composed of 102 amino acid residues. The phospholipase C activity of S-Hemolysin exhibited the specificities for the following substrates in the order ; lysophosphatidylethanolamine>sphingomyelin>phosphatidylethanolamine>phosphatidylcholine. S-Hemolysin showed the hemolytic activity against human erythrocytes. The strain also produced two kinds of phospholipase inhibitors, designated as SHI and S-PLI.The molecular weight of S-PLI was estimated to be 65,000 and the inhibitor was found to be a glycoprotein with a composition of 609 amino acids and 19 glucose residues. S-PLI is the first reported example of a glycoproteinaceous inhibitor of microbial origin which is able to specifically inhibit phospholipase C.SHI was shown to be a basic substance containing an amino group and glycoside moiety, and it was a more effective inhibitor of S-Hemolysin and sphingomyelinase.
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