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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 384 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 377 | - |
dc.citation.title | MOLECULES AND CELLS | - |
dc.citation.volume | 13 | - |
dc.contributor.author | Park, SK | - |
dc.contributor.author | Lee, JR | - |
dc.contributor.author | Lee, SS | - |
dc.contributor.author | Son, HJ | - |
dc.contributor.author | Yoo, JY | - |
dc.contributor.author | Moon, JC | - |
dc.contributor.author | Kwon, HY | - |
dc.contributor.author | Lim, CO | - |
dc.contributor.author | Bahk, JD | - |
dc.contributor.author | Cho, Moo Je | - |
dc.contributor.author | Lee, SY | - |
dc.date.accessioned | 2023-12-22T11:37:55Z | - |
dc.date.available | 2023-12-22T11:37:55Z | - |
dc.date.created | 2014-09-23 | - |
dc.date.issued | 2002-06 | - |
dc.description.abstract | Three soluble enzyme fractions (F-I, F-II, and F-III) that hydrolyze phophoinositides were separated from soybean sprouts by using Matrex green gel column chromatography. Among the three phosphatidylinositol (PI)-specific phopholipsase C (PLC) enzymes, only the third fraction (F-III) was able to hydrolyze phosphatidylinositol 4,5-bisphosphate (PIP2) as well as phosphatidylinositol (PI) and phosphatidylinositol phosphate (PIP) as substrates. The F-I and F-II fractions only showed enzymatic activities for PI and PIP. The PIP2-hydrolyzing PLC protein, F-III, was partially purified using the chromatographic steps of the Matrex green gel, phenyl Toyopearl, Matrex orange gel, Mono S cation exchange, and superose 6 gel filtration columns. The molecular weight of the F-III protein was estimated to be about 64 kDa on SDS-PAGE. The protein showed immunocross-reactivity with a polyclonal antibody that was prepared against the X and Y motifs of animal PLC enzymes, the conserved catalytic domains. Ca2+ ion critically affected the PIP2-hydrolyzing PLC activity of the F-III protein, representing maximal activity at 10 muM Ca2+ concentration. The PIP2-hydrolyzing PLC activity of the protein was also significantly increased by sodium deoxycholate (SDC) from 0.05 to 0.08%. However, the activity was greatly reduced above the concentration, and no activity was detected at 0.3% SDC. In addition, the protein exhibited maximal PIP2-hydrolyzing PLC activity at pH, in the range of 6.5-7.5. | - |
dc.identifier.bibliographicCitation | MOLECULES AND CELLS, v.13, no.3, pp.377 - 384 | - |
dc.identifier.issn | 1016-8478 | - |
dc.identifier.scopusid | 2-s2.0-1842858413 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/6359 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=1842858413 | - |
dc.identifier.wosid | 000176557400004 | - |
dc.language | 영어 | - |
dc.publisher | KOREAN SOC MOLECULAR & CELLULAR BIOLOGY | - |
dc.title | Partial purification and properties of a phosphatidylinositol 4,5-bisphosphate hydrolyzing phospholipase C from the soluble fraction of soybean sprouts | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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