dc.citation.endPage |
712 |
- |
dc.citation.number |
2 |
- |
dc.citation.startPage |
706 |
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dc.citation.title |
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS |
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dc.citation.volume |
194 |
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dc.contributor.author |
KIM, MJ |
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dc.contributor.author |
BAHK, YY |
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dc.contributor.author |
MIN, DS |
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dc.contributor.author |
LEE, SJ |
- |
dc.contributor.author |
RYU, SH |
- |
dc.contributor.author |
Suh, Pann-Ghill |
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dc.date.accessioned |
2023-12-22T13:06:27Z |
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dc.date.available |
2023-12-22T13:06:27Z |
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dc.date.created |
2014-09-03 |
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dc.date.issued |
1993-07 |
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dc.description.abstract |
Phospholipase C-β4(PLC-β4), a new member of phospholipase C isozyme, was purified from bovine cerebellum. The cDNA encoding rat PLC-β4 has been cloned from a cDNA library prepared from rat brain. The predicted open reading frame encodes a protein of 1,176 amino acids with a calculated molecular weight of 134,552. The deduced amino acid sequence exhibits 39, 36, and 36% identity with the sequences of rat PLC-β1, human PLC-β2, and rat PLC-β3, respectively. The amino acid sequence of PLC-β4, especially, shows higher identity (50%) with norpA PLC sequence from Drosophila melanogaster than those of other PLC-β subtypes, suggesting that the PLC-β4 might be a mammalian PLC equivalent of norpA PLC implicated in photosignal transduction in Drosophila. |
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dc.identifier.bibliographicCitation |
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.194, no.2, pp.706 - 712 |
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dc.identifier.doi |
10.1006/bbrc.1993.1879 |
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dc.identifier.issn |
0006-291X |
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dc.identifier.scopusid |
2-s2.0-0027312968 |
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dc.identifier.uri |
https://scholarworks.unist.ac.kr/handle/201301/5714 |
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dc.identifier.url |
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0027312968 |
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dc.identifier.wosid |
A1993LP96900018 |
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dc.language |
영어 |
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dc.publisher |
ACADEMIC PRESS INC ELSEVIER SCIENCE |
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dc.title |
CLONING OF CDNA-ENCODING RAT PHOSPHOLIPASE C-BETA-4, A NEW MEMBER OF THE PHOSPHOLIPASE-C |
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dc.type |
Article |
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dc.description.journalRegisteredClass |
scopus |
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