Identification of multiple forms of membrane-associated neutral sphingomyelinase in bovine brain
DC Field | Value | Language |
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dc.contributor.author | Jung, SY | - |
dc.contributor.author | Suh, JH | - |
dc.contributor.author | Park, HJ | - |
dc.contributor.author | Jung, KM | - |
dc.contributor.author | Kim, MY | - |
dc.contributor.author | Na, DS | - |
dc.contributor.author | Kim, DK | - |
dc.date.available | 2019-05-30T10:32:47Z | - |
dc.date.issued | 2000-09 | - |
dc.identifier.issn | 0022-3042 | - |
dc.identifier.issn | 1471-4159 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/25289 | - |
dc.description.abstract | Many different stimuli such as bioactive agents and environmental stresses are known to cause the activation of sphingomyelinase (SMase), which hydrolyzes sphingomyelin to generate ceramide as a second messenger playing a key role in differentiation and apoptosis in various cell types. Here we identified multiple forms of the membrane-associated neutral SMase (N-mSMase) activity in bovine brain. They could be classified into two groups according to extracting agents: group T-mSMase, extracted with 0.2% Triton X-100, and group S-mSMase, extracted with 0.5 M (NH4)(2)SO4. Group T-mSMase was further separated into four forms of T-mSMase: alpha, beta, gamma, and delta, which were extensively purified from 40,000-g pellets of bovine brain homogenates by 3,150-, 5,275-, 1,665- and 2,556-fold over the membrane extracts, respectively, by sequential use of several column chromatographies. On the other hand, S-mSMase was eluted as two active peaks of S-mSMase epsilon and zeta in a phenyl-5PW hydrophobic HPLC column and further purified by 1,119- and 976-fold over 40,000-g pellets of the homogenates, respectively. These highly purified N-mSMase enzyme preparations migrated as several bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and showed many different features in biochemical properties such as pH dependence, Mg2+ requirements, and effects of detergents. Taken together, our data strongly suggest that mammalian brain N-mSMase may exist as multiple forms different in both its chromatographic profiles and biochemical properties. | - |
dc.format.extent | 11 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | LIPPINCOTT WILLIAMS & WILKINS | - |
dc.title | Identification of multiple forms of membrane-associated neutral sphingomyelinase in bovine brain | - |
dc.type | Article | - |
dc.identifier.doi | 10.1046/j.1471-4159.2000.0751004.x | - |
dc.identifier.bibliographicCitation | JOURNAL OF NEUROCHEMISTRY, v.75, no.3, pp 1004 - 1014 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000088868500013 | - |
dc.identifier.scopusid | 2-s2.0-0033840568 | - |
dc.citation.endPage | 1014 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 1004 | - |
dc.citation.title | JOURNAL OF NEUROCHEMISTRY | - |
dc.citation.volume | 75 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordAuthor | neutral sphingomyelinase | - |
dc.subject.keywordAuthor | ceramide | - |
dc.subject.keywordAuthor | purification | - |
dc.subject.keywordAuthor | mammalian brain | - |
dc.subject.keywordPlus | HL-60 CELL-DIFFERENTIATION | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
dc.subject.keywordPlus | RAT-BRAIN | - |
dc.subject.keywordPlus | ACID SPHINGOMYELINASE | - |
dc.subject.keywordPlus | CERAMIDE | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | ALPHA | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Neurosciences & Neurology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Neurosciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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