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Enhanced sialylation and in vivo efficacy of recombinant human alpha-galactosidase through in vitro glycosylation : Enhanced sialylation and in vivo efficacy of recombinant human α-galactosidase through in vitro glycosylation
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Sohn, Youngsoo | - |
dc.contributor.author | Lee, Jung Mi | - |
dc.contributor.author | Park, Heung-Rok | - |
dc.contributor.author | Jung, Sung-Chul | - |
dc.contributor.author | Park, Tai Hyun | - |
dc.contributor.author | Oh, Doo-Byoung | - |
dc.creator | 박태현 | - |
dc.date.accessioned | 2013-08-14T00:50:48Z | - |
dc.date.available | 2013-08-14T00:50:48Z | - |
dc.date.created | 2018-07-09 | - |
dc.date.issued | 2013-03 | - |
dc.identifier.citation | BMB REPORTS, Vol.46 No.3, pp.157-162 | - |
dc.identifier.issn | 1976-6696 | - |
dc.identifier.uri | https://hdl.handle.net/10371/83296 | - |
dc.description.abstract | Human alpha-galactosidase A (GLA) has been used in enzyme replacement therapy for patients with Fabry disease. We expressed recombinant GLA from Chinese hamster ovary cells with very high productivity. When compared to an approved GLA (agalsidase beta), its size and charge were found to be smaller and more neutral. These differences resulted from the lack of terminal sialic acids playing essential roles in the serum half-life and proper tissue targeting. Because a simple sialylation reaction was not enough to increase the sialic acid content, a combined reaction using galactosyltransferase, sialyltransferase, and their sugar substrates at the same time was developed and optimized to reduce the incubation time. The product generated by this reaction had nearly the same size, isoelectric points, and sialic acid content as agalsidase beta. Furthermore, it had better in vivo efficacy to degrade the accumulated globotriaosylceramide in target organs of Fabry mice compared to an unmodified version. [BMB Reports 2013; 46(3): 157-162] | - |
dc.language | 영어 | - |
dc.language.iso | en | en |
dc.publisher | KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY | - |
dc.title | Enhanced sialylation and in vivo efficacy of recombinant human alpha-galactosidase through in vitro glycosylation | - |
dc.title.alternative | Enhanced sialylation and in vivo efficacy of recombinant human α-galactosidase through in vitro glycosylation | - |
dc.type | Article | - |
dc.author.alternative | 손영수 | - |
dc.author.alternative | 이정미 | - |
dc.author.alternative | 박흥록 | - |
dc.author.alternative | 정성철 | - |
dc.author.alternative | 박태현 | - |
dc.author.alternative | 오두병 | - |
dc.identifier.doi | 10.5483/BMBRep.2013.46.3.192 | - |
dc.citation.journaltitle | BMB REPORTS | - |
dc.identifier.wosid | 000318073700004 | - |
dc.identifier.scopusid | 2-s2.0-84876861105 | - |
dc.description.srnd | OAIID:oai:osos.snu.ac.kr:snu2013-01/102/0000002410/7 | - |
dc.description.srnd | SEQ:7 | - |
dc.description.srnd | PERF_CD:SNU2013-01 | - |
dc.description.srnd | EVAL_ITEM_CD:102 | - |
dc.description.srnd | USER_ID:0000002410 | - |
dc.description.srnd | ADJUST_YN:Y | - |
dc.description.srnd | EMP_ID:A002014 | - |
dc.description.srnd | DEPT_CD:458 | - |
dc.description.srnd | CITE_RATE:1.718 | - |
dc.description.srnd | FILENAME:enhanced sialylation and in vivo efficacy of.pdf | - |
dc.description.srnd | DEPT_NM:화학생물공학부 | - |
dc.description.srnd | EMAIL:thpark@snu.ac.kr | - |
dc.description.srnd | SCOPUS_YN:Y | - |
dc.description.srnd | CONFIRM:Y | - |
dc.citation.endpage | 162 | - |
dc.citation.number | 3 | - |
dc.citation.startpage | 157 | - |
dc.citation.volume | 46 | - |
dc.identifier.kciid | ART001752691 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Park, Tai Hyun | - |
dc.identifier.srnd | 2013-01/102/0000002410/7 | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | alpha galactosidase | - |
dc.subject.keywordPlus | n acetylneuraminic acid | - |
dc.subject.keywordPlus | recombinant protein | - |
dc.subject.keywordPlus | animal | - |
dc.subject.keywordPlus | article | - |
dc.subject.keywordPlus | CHO cell | - |
dc.subject.keywordPlus | glycosylation | - |
dc.subject.keywordPlus | hamster | - |
dc.subject.keywordPlus | human | - |
dc.subject.keywordPlus | in vitro study | - |
dc.subject.keywordPlus | isoelectric point | - |
dc.subject.keywordPlus | metabolism | - |
dc.subject.keywordPlus | polyacrylamide gel electrophoresis | - |
dc.subject.keywordPlus | alpha-Galactosidase | - |
dc.subject.keywordPlus | Animals | - |
dc.subject.keywordPlus | CHO Cells | - |
dc.subject.keywordPlus | Cricetinae | - |
dc.subject.keywordPlus | Electrophoresis, Polyacrylamide Gel | - |
dc.subject.keywordPlus | Glycosylation | - |
dc.subject.keywordPlus | Humans | - |
dc.subject.keywordPlus | Isoelectric Point | - |
dc.subject.keywordPlus | N-Acetylneuraminic Acid | - |
dc.subject.keywordPlus | Recombinant Proteins | - |
dc.subject.keywordPlus | Cricetulus griseus | - |
dc.subject.keywordPlus | Mus | - |
dc.subject.keywordAuthor | Alpha-galactosidase A | - |
dc.subject.keywordAuthor | Enzyme replacement therapy | - |
dc.subject.keywordAuthor | Fabry disease | - |
dc.subject.keywordAuthor | In vitro glycosylation | - |
dc.subject.keywordAuthor | Sialic acid | - |
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