| Project/Area Number |
06671833
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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 |
Morphological basic dentistry
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| Research Institution | TOKYO DENTAL COLLEGE |
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Principal Investigator |
ISHIHARA Kazuyuki Tokyo Dental College, Assistant Proffessor, 歯学部・微生物学講座, 講師 (00212910)
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| Co-Investigator(Kenkyū-buntansha) |
KATO Testuo Tokyo Dental College, Associate Proffessor, 歯学部・微生物学講座, 助教授 (00159253)
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| Project Period (FY) |
1994 – 1995
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| Project Status |
Completed (Fiscal Year 1995)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1995: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1994: ¥1,300,000 (Direct Cost: ¥1,300,000)
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| Keywords | Treponema denticola / Serine protease / Cloning / Sequence / Pathogen / Periodontitis / Cell surface protein / Treponema dinticola / protease / cloning / sequence / pathogen |
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| Research Abstract |
A proline-phenylalanine specific protease from Treponema denticola ATCC35405 was purified by conventional column technique. From the inhibitor assay, this protease was classified as a serine protease. Internal protease inhibitors such as al-antitrypsin and al-antichymotrypsin have no effect on the enzymatic activity. The enzyme completely degrades fibronectin, al-antitrypsin, and gelatin and partially degrades immunoglobulin G heavy chain and type IV collagen. The purified enzyme consists of three polypeptides. NH_2-terminal amino acid sequence were determined from purified enzyme. Based on the sequences, the protease gene was cloned and sequenced. The open reading frame consists of 2,169bp and codes for a protein with a Mr of approximately 70kDa. This protein consist of signal peptide region, NH_2-terminal prosequence and mature protease domain. The expressed protein did not posessed proteolytic activity, however, the antibody against T.denticola whole cell react the protein. The deduced amino acid sequence showed its homology with a serine protease.
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