dc.citation.endPage |
196 |
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dc.citation.number |
1 |
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dc.citation.startPage |
189 |
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dc.citation.title |
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS |
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dc.citation.volume |
174 |
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dc.contributor.author |
KIM, DK |
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dc.contributor.author |
Suh, Pann-Ghill |
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dc.contributor.author |
RYU, SH |
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dc.date.accessioned |
2023-12-22T13:08:46Z |
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dc.date.available |
2023-12-22T13:08:46Z |
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dc.date.created |
2014-09-03 |
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dc.date.issued |
1991-01 |
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dc.description.abstract |
An intracellular form of phospholipase A2 was purified about 47,500-fold to near homogeneity from bovine platelets 100,000 × g supernatant by sequential use of column chromatographies on Heparin-Sepharose, DEAE-Sephacel, Butyl-Toyopearl, Sephacryl S-300, DEAE-5PW HPLC, TSK G 3000 SW HPLC and Mono Q FPLC. The final preparation showed a single band on SDS-polyacrylamide gel, and its molecular mass was estimated to be approximately 100,000 daltons. The purified PLA2 showed maximal activity at alkaline pH(pH 9.0-10.0) and considerable activity at 0.3-1.0μM calcium concentration. It hydrolyzed phosphatidylcholine containing arachidonate at sn-2 position with high selectivity in comparison to linoleate. |
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dc.identifier.bibliographicCitation |
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.174, no.1, pp.189 - 196 |
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dc.identifier.doi |
10.1016/0006-291X(91)90504-Z |
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dc.identifier.issn |
0006-291X |
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dc.identifier.scopusid |
2-s2.0-0025963999 |
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dc.identifier.uri |
https://scholarworks.unist.ac.kr/handle/201301/5716 |
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dc.identifier.url |
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0025963999 |
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dc.identifier.wosid |
A1991ET20700030 |
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dc.language |
영어 |
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dc.publisher |
ACADEMIC PRESS INC ELSEVIER SCIENCE |
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dc.title |
PURIFICATION AND SOME PROPERTIES OF A PHOSPHOLIPASE-A2 FROM BOVINE PLATELETS |
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dc.type |
Article |
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dc.description.journalRegisteredClass |
scopus |
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