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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 446 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 441 | - |
dc.citation.title | PROTEIN EXPRESSION AND PURIFICATION | - |
dc.citation.volume | 41 | - |
dc.contributor.author | Kim, Yu-Jin | - |
dc.contributor.author | Park, Sunghoon | - |
dc.contributor.author | Oh, You-Kwan | - |
dc.contributor.author | Kang, Whankoo | - |
dc.contributor.author | Kim, Hee Sook | - |
dc.contributor.author | Lee, Eun Yeol | - |
dc.date.accessioned | 2023-12-22T10:36:14Z | - |
dc.date.available | 2023-12-22T10:36:14Z | - |
dc.date.created | 2017-03-04 | - |
dc.date.issued | 2005-06 | - |
dc.description.abstract | Caseinomacropeptide (CMP) is a biologically active polypeptide derived from the C-terminal Of milk K-casein. CMP is heterogeneous since it is modified differently by glycosylation and phosphorylation after translation. Recently, recombinant human CMP (hCMP) has been produced as a secretory product in yeast. The present Study aimed at the purification and characterization of recombinant hCMP. By sequential molecular cut-off ultrafiltration and anion-exchange chromatography, the recombinant hCMP in the culture broth could be purified to an HPLC purity over 94 %. The authenticity of the purified hCMP was confirmed by sequence analysis of N-terminal amino acids. The recombinant hCMP was estimated to be 7.0 kDa by SDS-PAGE, and showed a lower glycosylation than the natural bovine CMP. | - |
dc.identifier.bibliographicCitation | PROTEIN EXPRESSION AND PURIFICATION, v.41, no.2, pp.441 - 446 | - |
dc.identifier.doi | 10.1016/j.pep.2005.02.021 | - |
dc.identifier.issn | 1046-5928 | - |
dc.identifier.scopusid | 2-s2.0-18144386191 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/25378 | - |
dc.identifier.url | http://www.sciencedirect.com/science/article/pii/S1046592805000732 | - |
dc.identifier.wosid | 000229192800026 | - |
dc.language | 영어 | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.title | Purification and characterization of human caseinomacropeptide produced by a recombinant Saccharomyces cerevisiae | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Caseinomacropeptide | - |
dc.subject.keywordAuthor | Saccharomyces cerevisiae | - |
dc.subject.keywordAuthor | ultrafiltration | - |
dc.subject.keywordAuthor | anion-exchange chromatography | - |
dc.subject.keywordAuthor | O-glycosylation | - |
dc.subject.keywordPlus | CASEIN MACROPEPTIDE | - |
dc.subject.keywordPlus | O-GLYCOSYLATION | - |
dc.subject.keywordPlus | K-CASEIN | - |
dc.subject.keywordPlus | GLYCOMACROPEPTIDE | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | YEAST | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | RAT | - |
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