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https://ahro.austin.org.au/austinjspui/handle/1/9462
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DC Field | Value | Language |
---|---|---|
dc.contributor.author | McQueen, Kim | en |
dc.contributor.author | Kovac, Suzana | en |
dc.contributor.author | Ho, Po-Ki | en |
dc.contributor.author | Rorison, Kristy | en |
dc.contributor.author | Pannequin, Julie | en |
dc.contributor.author | Neumann, Greg | en |
dc.contributor.author | Shulkes, Arthur | en |
dc.contributor.author | Baldwin, Graham S | en |
dc.date.accessioned | 2015-05-15T22:34:01Z | |
dc.date.available | 2015-05-15T22:34:01Z | |
dc.date.issued | 2002-10-01 | en |
dc.identifier.citation | Journal of Protein Chemistry; 21(7): 465-71 | en |
dc.identifier.govdoc | 12523650 | en |
dc.identifier.other | PUBMED | en |
dc.identifier.uri | https://ahro.austin.org.au/austinjspui/handle/1/9462 | en |
dc.description.abstract | The bacterial expression of human progastrin(6-80) has been reported previously [Baldwin, G.S. et al. (2001) J. Biol. Chem. 276: 7791-7796]. The aims of the present study were to prepare full-length recombinant human progastrin(1-80) and to compare its biological activity with that of progastrin(6-80) in vitro, to determine whether or not the N-terminal five amino acids contributed to activity. A fusion protein of glutathione-S-transferase and human progastrin(1-80) was expressed in Escherichia coli, collected on glutathione-agarose beads, and cleaved with enterokinase. Progastrin(1-80) was purified by reversed-phase and anion exchange HPLC and characterized by radioimmunoassay, amino acid sequencing, and mass spectrometry. No differences were detected in the extent of stimulation by progastrin(1-80) and progastrin(6-80) in proliferation and migration assays with the mouse gastric cell line IMGE-5. We conclude that residues 1-5 of progastrin(1-80) are not essential for biological activity. | en |
dc.language.iso | en | en |
dc.subject.other | Amino Acid Sequence | en |
dc.subject.other | Amino Acids.analysis | en |
dc.subject.other | Animals | en |
dc.subject.other | Cell Division.drug effects | en |
dc.subject.other | Cell Line, Transformed | en |
dc.subject.other | Cell Movement.drug effects | en |
dc.subject.other | Chromatography, High Pressure Liquid.methods | en |
dc.subject.other | Escherichia coli.genetics.metabolism | en |
dc.subject.other | Gastric Mucosa.cytology | en |
dc.subject.other | Gastrins.biosynthesis.genetics.pharmacology | en |
dc.subject.other | Glutathione Transferase.genetics | en |
dc.subject.other | Humans | en |
dc.subject.other | Mice | en |
dc.subject.other | Mice, Transgenic | en |
dc.subject.other | Molecular Sequence Data | en |
dc.subject.other | Protein Precursors.biosynthesis.genetics.pharmacology | en |
dc.subject.other | Radioimmunoassay | en |
dc.subject.other | Recombinant Fusion Proteins.biosynthesis.genetics.pharmacology | en |
dc.subject.other | Spectrometry, Mass, Electrospray Ionization | en |
dc.title | Preparation of biologically active recombinant human progastrin(1-80). | en |
dc.type | Journal Article | en |
dc.identifier.journaltitle | Journal of protein chemistry | en |
dc.identifier.affiliation | University of Melbourne Department of Surgery, Austin and Repatriation Medical Centre, Melbourne, Victoria, Australia | en |
dc.description.pages | 465-71 | en |
dc.relation.url | https://pubmed.ncbi.nlm.nih.gov/12523650 | en |
dc.type.austin | Journal Article | en |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.fulltext | No Fulltext | - |
item.grantfulltext | none | - |
item.languageiso639-1 | en | - |
item.openairetype | Journal Article | - |
Appears in Collections: | Journal articles |
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