DC Field | Value | Language |
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dc.contributor.author | H G Kim | - |
dc.contributor.author | S M Yang | - |
dc.contributor.author | Y C Lee | - |
dc.contributor.author | Su Il Do | - |
dc.contributor.author | I S Chung | - |
dc.contributor.author | J M Yang | - |
dc.date.accessioned | 2017-04-19T08:59:58Z | - |
dc.date.available | 2017-04-19T08:59:58Z | - |
dc.date.issued | 2003 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | 10.1016/S0006-291X(03)00795-2 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/6145 | - |
dc.description.abstract | cDNAs, encoding human β1,4-galactosyltransferase (hGalT I, EC 2.4.1.22), human Galβ1,3(4)-GlcNAc α2,3-sialyltransferase (hST3GalIII, EC 2.4.99), and human Galβ1,4-GlcNAc α2,6-sialyltransferase (hST6Gal I, EC 2.4.99.1), were cloned from human cell lines. In order to express these glycosyltransferases as secreted form in insect cells, cDNAs were inserted into a novel baculovirus transfer vector equipped with the mouse IgM signal peptide and IgG binding domain of the Staphylococcus aureus protein A as an N-terminal fusion partner. About 14mg hGalT I, 8mg hST3GalIII, and 6.4mg hST6Gal I were purified from 1liter of recombinant baculovirus infected insect cell culture media. The specific activities of recombinant hGalT I and hST6Gal I were determined as 0.65 and 1.6U/mg protein, respectively. These results indicated that the recombinant hGalT I and hST6Gal I retained enzyme activities at similar level to those of the authentic one although they were fused with the IgG binding domain at the N-terminus. Taken together, the mouse IgM signal peptide and IgG binding domain of the protein A could be efficiently used as an N-terminus fusion partner for the over-expression of heterologous proteins in insect cells. | - |
dc.publisher | Elsevier | - |
dc.title | High-level expression of human glycosyltransferases in insect cells as biochemically active form | - |
dc.title.alternative | High-level expression of human glycosyltransferases in insect cells as biochemically active form | - |
dc.type | Article | - |
dc.citation.title | Biochemical and Biophysical Research Communications | - |
dc.citation.number | 3 | - |
dc.citation.endPage | 493 | - |
dc.citation.startPage | 488 | - |
dc.citation.volume | 305 | - |
dc.contributor.affiliatedAuthor | Su Il Do | - |
dc.contributor.alternativeName | 김형구 | - |
dc.contributor.alternativeName | 양승모 | - |
dc.contributor.alternativeName | 이영춘 | - |
dc.contributor.alternativeName | 도수일 | - |
dc.contributor.alternativeName | 정인식 | - |
dc.contributor.alternativeName | 양재명 | - |
dc.identifier.bibliographicCitation | Biochemical and Biophysical Research Communications, vol. 305, no. 3, pp. 488-493 | - |
dc.identifier.doi | 10.1016/S0006-291X(03)00795-2 | - |
dc.subject.keyword | Galactosyltransferase | - |
dc.subject.keyword | Heterologous expression | - |
dc.subject.keyword | IgM signal peptide | - |
dc.subject.keyword | Insect cell | - |
dc.subject.keyword | Protein A | - |
dc.subject.keyword | Sialyltransferase | - |
dc.subject.local | Galactosyltransferase | - |
dc.subject.local | heterologous expression | - |
dc.subject.local | Heterologous expression | - |
dc.subject.local | IgM signal peptide | - |
dc.subject.local | Insect cells | - |
dc.subject.local | insect cell | - |
dc.subject.local | Insect cell | - |
dc.subject.local | Protein A | - |
dc.subject.local | Sialyltransferase | - |
dc.subject.local | sialyltransferase | - |
dc.description.journalClass | Y | - |
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