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Article: Expression of recombinant human glucose-dependent insulinotropic polypeptide in Escherichia coli by sequence-specific proteolysis of a protein A fusion protein

TitleExpression of recombinant human glucose-dependent insulinotropic polypeptide in Escherichia coli by sequence-specific proteolysis of a protein A fusion protein
Authors
Issue Date1990
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/peptides
Citation
Peptides, 1990, v. 11 n. 6, p. 1069-1074 How to Cite?
AbstractGlucose-dependent insulinotropic polypeptide (GIP) is a forty-two amino acid hormone that stimulates the secretion of insulin from the pancreatic B-cells in the presence of elevated glucose concentrations. The human GIP gene with the human Aα-fibrinopeptide sequence was synthesized and linked to the Staphylococcus aureus protein A gene in the vector pRIT2T. This plasmid was expressed in Escherichia coli, and the resulting fusion protein consisted of three domains: protein A for ease of purification, fibrinopeptide sequence for thrombin cleavage and human GIP. The GIP was subsequently cleaved from the fusion protein with α-thrombin. The identity of the recombinant human GIP was confirmed by SDS-PAGE, ELISA, HPLC and amino-terminal amino acid sequence analysis. This recombinant product was shown to have comparable insulinotropic activity to porcine GIP in the isolated perfused pancreas.
Persistent Identifierhttp://hdl.handle.net/10722/178501
ISSN
2015 Impact Factor: 2.535
2015 SCImago Journal Rankings: 1.128
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChow, BKCen_US
dc.contributor.authorMorrow, GWen_US
dc.contributor.authorHo, Men_US
dc.contributor.authorPederson, RAen_US
dc.contributor.authorMcintosh, CHSen_US
dc.contributor.authorBrown, JCen_US
dc.contributor.authorMacgillivray, RTAen_US
dc.date.accessioned2012-12-19T09:48:03Z-
dc.date.available2012-12-19T09:48:03Z-
dc.date.issued1990en_US
dc.identifier.citationPeptides, 1990, v. 11 n. 6, p. 1069-1074en_US
dc.identifier.issn0196-9781en_US
dc.identifier.urihttp://hdl.handle.net/10722/178501-
dc.description.abstractGlucose-dependent insulinotropic polypeptide (GIP) is a forty-two amino acid hormone that stimulates the secretion of insulin from the pancreatic B-cells in the presence of elevated glucose concentrations. The human GIP gene with the human Aα-fibrinopeptide sequence was synthesized and linked to the Staphylococcus aureus protein A gene in the vector pRIT2T. This plasmid was expressed in Escherichia coli, and the resulting fusion protein consisted of three domains: protein A for ease of purification, fibrinopeptide sequence for thrombin cleavage and human GIP. The GIP was subsequently cleaved from the fusion protein with α-thrombin. The identity of the recombinant human GIP was confirmed by SDS-PAGE, ELISA, HPLC and amino-terminal amino acid sequence analysis. This recombinant product was shown to have comparable insulinotropic activity to porcine GIP in the isolated perfused pancreas.en_US
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/peptidesen_US
dc.relation.ispartofPeptidesen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBiological Assayen_US
dc.subject.meshEscherichia Coli - Metabolismen_US
dc.subject.meshGastric Inhibitory Polypeptide - Biosynthesisen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPancreas - Chemistryen_US
dc.subject.meshPerfusionen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Inbred Strainsen_US
dc.subject.meshRecombinant Fusion Proteins - Metabolismen_US
dc.subject.meshRecombinant Proteins - Biosynthesisen_US
dc.subject.meshStaphylococcal Protein A - Metabolismen_US
dc.subject.meshSubstrate Specificityen_US
dc.subject.meshThrombinen_US
dc.titleExpression of recombinant human glucose-dependent insulinotropic polypeptide in Escherichia coli by sequence-specific proteolysis of a protein A fusion proteinen_US
dc.typeArticleen_US
dc.identifier.emailChow, BKC: bkcc@hku.hken_US
dc.identifier.authorityChow, BKC=rp00681en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0196-9781(90)90132-Oen_US
dc.identifier.pmid2087431-
dc.identifier.scopuseid_2-s2.0-0025634263en_US
dc.identifier.volume11en_US
dc.identifier.issue6en_US
dc.identifier.spage1069en_US
dc.identifier.epage1074en_US
dc.identifier.isiWOS:A1990EQ00800003-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChow, BKC=7102826193en_US
dc.identifier.scopusauthoridMorrow, GW=7102277890en_US
dc.identifier.scopusauthoridHo, M=7403080604en_US
dc.identifier.scopusauthoridPederson, RA=7005815440en_US
dc.identifier.scopusauthoridMcIntosh, CHS=7103076827en_US
dc.identifier.scopusauthoridBrown, JC=7409452569en_US
dc.identifier.scopusauthoridMacGillivray, RTA=7004286039en_US

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