1996 Fiscal Year Final Research Report Summary
Elucidation of Hemolytic Structure of novel Phospholipase C produced by Microorganizm.
| Project/Area Number |
07660115
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | Kumamoto University |
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Principal Investigator |
UYEDA Masaru Kumamoto University, Pharmaceutical Sciences, Professor., 薬学部, 教授 (80038231)
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| Co-Investigator(Kenkyū-buntansha) |
SUZUKI Keitarou Kumamoto University, Pharmaceutical Sciences, Assistant professor., 薬学部, 助教授 (10154535)
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| Project Period (FY) |
1995 – 1996
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| Keywords | phospholipase / S-Hemolysin / Streptomyces sp. / inhibitor / S-PLI / SHI / sphingomyelinase / glycoprotein |
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| 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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