ArticleJournal of protein chemistry2002
Preparation of biologically active recombinant human progastrin(1-80).
Article in Journal of protein chemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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0 citing papers in PubMed, 9 citations in OpenAlex.
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8 authors at 3 institutions in 1 country.
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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.
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