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- W100296593 abstract "Glucokinase (GK) is a member of a superfamily of hexokinases that phosphorylates glucose to glucose-6-phosphate and is modulated by a regulatory protein (GKRP), with association of the inhibitory complex occurring in the presence of fructose-6-phosphate (F6P) and dissociation promoted in the presence of fructose-1-phosphate (F1P). Using complementary single-stranded synthetic oligonucleotides to construct duplex DNA corresponding to the unique 3′-terminus of β-islet mRNA splicing variant, the chimeric gene was subcloned and overexpressed in E. coli yielding the putative β 1-GKRP isoform produced in pancreatic β-islet cells as described by Alvarez, et al. After purification of β 1-GKRP by metal chelation affinity chromatography, the variant protein was tested for its ability to bind and inhibit human liver glucokinase. A qualitative differential binding assay was developed using a chitin binding domain/glucokinase (CBD/GK) fusion protein immobilized on a chitin column as bait against β 1-GKRP as the mobile phase. Also, the inhibition of GK by B1-GKRP in the presence of either F6P or F1P was observed and compared to that of rat liver GKRP by monitoring glucokinase activity as coupled to either pyruvate kinase/ lactate dehydrogenase or glucose-6-phosphate dehydrogenase activity. Andrew W. Mellon Faculty Career Enhancement" @default.
- W100296593 created "2016-06-24" @default.
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- W100296593 date "2006-03-01" @default.
- W100296593 modified "2023-09-27" @default.
- W100296593 title "Expression and Characterization of the β 1 Isoform of Glucokinase Regulatory Protein (GKRP) from Homo sapiens β‐Islet Cells" @default.
- W100296593 doi "https://doi.org/10.1096/fasebj.20.5.a955" @default.
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