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DC Field | Value | Language |
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dc.citation.endPage | 6653 | - |
dc.citation.number | 19 | - |
dc.citation.startPage | 6649 | - |
dc.citation.title | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | - |
dc.citation.volume | 84 | - |
dc.contributor.author | RYU, SH | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | CHO, KS | - |
dc.contributor.author | LEE, KY | - |
dc.contributor.author | RHEE, SG | - |
dc.date.accessioned | 2023-12-22T13:11:11Z | - |
dc.date.available | 2023-12-22T13:11:11Z | - |
dc.date.created | 2015-08-17 | - |
dc.date.issued | 1987-10 | - |
dc.description.abstract | We previously reported that cytosolic fractions of bovine brain contain two immunologically distinct forms of phospholipase C (PLC), PLC-I and PLC-II. We now report the purification of another form of inositolphospholipid-specific phospholipase C from bovine brain cytosol, designated PLC-III, and the comparison of the catalytic properties of the three isozymes. Approximately 450 micrograms of pure PLC-III was obtained from 36 bovine brains, and it had a final specific activity of 30-40 mumol of phosphatidylinositol hydrolyzed per min per mg of enzyme in the presence of 0.1% deoxycholate. PLC-III exhibited an apparent Mr of 85,000 in NaDodSO4/PAGE, which is considerably smaller than the Mr of 150,000 for PLC-I and 145,000 for PLC-II. Neither of the two mixtures of monoclonal antibodies nor the rabbit polyclonal antibodies directed against either PLC-I or PLC-II cross-reacted with PLC-III. The catalytic properties of the three isozymes were studied by using small unilamellar vesicles prepared from either phosphatidylinositol (PtdIns) or phosphatidylinositol 4,5-bisphosphate (PtdInsP2) as substrates. Hydrolysis of both PtdIns and PtdInsP2 by the three enzymes was dependent on Ca2+. However, at low Ca2+ concentration, PtdInsP2 was the preferred substrate for all three enzymes. When PtdIns was the substrate, the three enzymes exhibited similar specific activities at their optimum pH, which was 4.8 for PLC-I, 5.0 for PLC-II, and 5.5 for PLC-III. But at neutral pH, the order of specific activity was PLC-III greater than PLC-II greater than PLC-I. In contrast, the order of specific activity was PLC-I greater than PLC-III greater than PLC-II for PtdInsP2 hydrolysis, which means that PLC-I is the most specific for PtdInsP2. The three enzymes were affected differently by bovine serum albumin: inhibition of PLC-I and activation of PLC-III were observed, whereas PLC-II was unaffected. This observation suggests that any putative protein effectors for PLC should be critically scrutinized. | - |
dc.identifier.bibliographicCitation | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.84, no.19, pp.6649 - 6653 | - |
dc.identifier.doi | 10.1073/pnas.84.19.6649 | - |
dc.identifier.issn | 0027-8424 | - |
dc.identifier.scopusid | 2-s2.0-0023427097 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/16536 | - |
dc.identifier.url | http://www.pnas.org/content/84/19/6649 | - |
dc.identifier.wosid | A1987K314300009 | - |
dc.language | 영어 | - |
dc.publisher | NATL ACAD SCIENCES | - |
dc.title | BOVINE BRAIN CYTOSOL CONTAINS 3 IMMUNOLOGICALLY DISTINCT FORMS OF INOSITOLPHOSPHOLIPID-SPECIFIC PHOSPHOLIPASE-C | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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