Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/63758
DC FieldValueLanguage
dc.contributorDepartment of Applied Biology and Chemical Technology-
dc.creatorLiu, P-
dc.creatorTian, GL-
dc.creatorLee, KS-
dc.creatorWong, MS-
dc.creatorYe, YH-
dc.date.accessioned2017-02-09T08:30:31Z-
dc.date.available2017-02-09T08:30:31Z-
dc.identifier.issn0040-4039-
dc.identifier.urihttp://hdl.handle.net/10397/63758-
dc.language.isoenen_US
dc.publisherPergamon Pressen_US
dc.subjectFull enzymatic synthesisen_US
dc.subjectOGP(10-14)en_US
dc.subjectProteaseen_US
dc.subjectOrganic solventen_US
dc.titleFull enzymatic synthesis of a precursor of bioactive pentapeptide OGP(10-14) in organic solventsen_US
dc.typeJournal/Magazine Articleen_US
dc.identifier.spage2423-
dc.identifier.epage2425-
dc.identifier.volume43-
dc.identifier.issue13-
dc.identifier.doi10.1016/S0040-4039(02)00278-2-
dcterms.abstractFull enzymatic synthesis of a fragment of osteogenic growth peptide (OGP), a precursor of bioactive pentapeptide OGP(10-14) (Z-TyrGlyPheGlyGlyOEt), was accomplished by papain, α-chymotrypsin, and thermolysin via 2+3 or 3+2 synthetic routes in organic solvents for the first time. The factors influencing the enzymatic synthesis of fragments of OGP(10-14) were systematically studied.-
dcterms.bibliographicCitationTetrahedron letters, 2002, v. 43, no. 13, p. 2423-2425-
dcterms.isPartOfTetrahedron letters-
dcterms.issued2002-
dc.identifier.eissn1873-3581-
dc.identifier.rosgroupidr10208-
dc.description.ros2001-2002 > Academic research: refereed > Publication in refereed journal-
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