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Structural Basis for the Biological Activities of Bovine Seminal Ribonuclease
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Jin-Soo | - |
dc.contributor.author | Soucek, Josef | - |
dc.contributor.author | Matousek, Josef | - |
dc.contributor.author | Raines, Ronald T. | - |
dc.date.accessioned | 2020-04-27T12:25:53Z | - |
dc.date.available | 2020-04-27T12:25:53Z | - |
dc.date.created | 2020-04-08 | - |
dc.date.created | 2020-04-08 | - |
dc.date.issued | 1995-05 | - |
dc.identifier.citation | Journal of Biological Chemistry, Vol.270 No.18, pp.10525-10530 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.other | 95223 | - |
dc.identifier.uri | https://hdl.handle.net/10371/165592 | - |
dc.description.abstract | Bovine seminal ribonuclease (BS-RNase) is a homolog of RNase A with special biological properties that include specific antitumor, aspermatogenic, and immunosuppressive activities. Unlike RNase A, BS-RNase is a dimer cross-linked by disulfide bonds between Cys(31) of one subunit and Cys(32) Of the other. At equilibrium, this dimer is a mixture of two distinct quaternary forms, M=M and MxM. The conversion of M=M to MxM entails the exchange of NH2-terminal alpha-helices between subunits. Here, the cytotoxic activities of purified MxM were shown to be greater than those of purified M=M, despite extensive equilibration of M=M and MxM during the time course of the assays. Replacing Cys(31) or Cys(32) with a serine residue did not compromise the enzymatic activity of dimeric BS-RNase, but reduced both the fraction of MxM at equilibrium and the cytotoxicity. We conclude that the MxM form is responsible for the special biological properties of BS-RNase. Since cytosolic ribonuclease inhibitor binds tightly to monomeric but not dimeric BS-RNase and only the MxM form can remain dimeric in the reducing environment of the cytosol, we propose that BS-RNase has evolved its MxM form to retain its lethal enzymatic activity in vivo. | - |
dc.language | 영어 | - |
dc.publisher | American Society for Biochemistry and Molecular Biology Inc. | - |
dc.title | Structural Basis for the Biological Activities of Bovine Seminal Ribonuclease | - |
dc.type | Article | - |
dc.contributor.AlternativeAuthor | 김진수 | - |
dc.identifier.doi | 10.1074/jbc.270.18.10525 | - |
dc.citation.journaltitle | Journal of Biological Chemistry | - |
dc.identifier.wosid | A1995QW60100027 | - |
dc.identifier.scopusid | 2-s2.0-0028932601 | - |
dc.citation.endpage | 10530 | - |
dc.citation.number | 18 | - |
dc.citation.startpage | 10525 | - |
dc.citation.volume | 270 | - |
dc.identifier.sci | A1995QW60100027 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Kim, Jin-Soo | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | AMINO-ACID-SEQUENCE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | RNASE | - |
dc.subject.keywordPlus | INVITRO | - |
dc.subject.keywordPlus | PLASMA | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | FLUID | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | TUMOR | - |
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