Please use this identifier to cite or link to this item:
Scopus Web of Science® Altmetric
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPolyak, S.-
dc.contributor.authorForsberg, G.-
dc.contributor.authorForbes, B.-
dc.contributor.authorMcNeil, K.-
dc.contributor.authorAplin, S.-
dc.contributor.authorWallace, J.-
dc.identifier.citationProtein Engineering Design and Selection, 1997; 10(6):615-619-
dc.description.abstractTo improve site-specific cleavage of a methionyl porcine growth hormone [[Met1]-pGH(1-46)-IGF-II] fusion protein by the enzyme H64A subtilisin, a series of flexible, unstructured spacer peptides were introduced N-terminal to the cleavage site. When enzymatic digestion preceded refolding of the fusion proteins, IGF-II could only be liberated from substrates which contained spacer peptides. Compared with the parent construct, the yield of IGF-II from refolded fusion proteins containing spacers was improved up to two-fold. Furthermore, this cleavage rate was improved by removing a competing protease recognition motif from the fusion partner. These data show that fusion partners can influence site-specific proteolysis of fusion proteins. Introduction of flexible spacers between the moieties can alleviate these interactions.-
dc.description.statementofresponsibilitySteve W Polyak, Göran Forsberg, Briony E Forbes, Kerrie A McNeil, Sally E Aplin, and John C Wallace-
dc.publisherOxford University Press-
dc.subjectGrowth Hormone-
dc.subjectInsulin-Like Growth Factor II-
dc.subjectProtein Sorting Signals-
dc.subjectRecombinant Proteins-
dc.subjectRecombinant Fusion Proteins-
dc.subjectMutagenesis, Site-Directed-
dc.subjectAmino Acid Sequence-
dc.subjectProtein Folding-
dc.subjectMolecular Sequence Data-
dc.titleIntroduction of spacer peptides N-terminal to a cleavage recognition motif in recombinant fusion proteins can improve site-specific cleavage-
dc.typeJournal article-
dc.identifier.orcidPolyak, S. [0000-0002-8458-5194]-
Appears in Collections:Aurora harvest 7
Biochemistry publications

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.