activity of recombinant enzyme towards glucose 1-phosphate shown to be 4.8fold higher than activity towards myo-inositol hexakisphosphate (phytate), kinetic parameters affected by entrapment of the enzyme in alginate beads
specific activities of recombinant enzymes similar to those of wild-type towards myo-inositol hexakisphosphate (i.e. phytate) and glucose 1-phosphate as substrates, entrapment in alginate beads, free enzyme looses less than 5% phosphatase activity within 2 h in 20 mM Tris-HCl buffer, pH 8.0, transfer limitation is responsible for the reduced reaction rate of the entrapped enzyme, complete conversion of myo-inositol hexakisphosphate into one single myo-inositol pentakisphosphate isomer, identified as D-myo-inositol(1,2,4,5,6)pentakisphosphate, shown to be feasible by using the enzyme-loaded alginate beads in batch operations
activities of free and entrapped enzyme determined at, dephosphorylation of myo-inositol hexakisphosphate (phytate) increases with raising temperature, compared to the free-form activity, reaction rate of the alginate reactor is markedly reduced, 30-75% depending on temperature
enzyme form GP2 present in the fat body; gel filtration Sephadex G-75, G100, ion-exchange chromatography on ADP-Sepharose, preparative isoelectrofocusing with Ampholines, preparative electrophoresis in blocks of polyacrylamide gel
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determination of crystal structure by multiwavelength anomalous dispersion using a tungstate derivate together with the H18A inactive mutant complex structure with D-glucose 1-phosphate at 2.4 A resolution
Utilization of exogenous glucose-1-phosphate as a source of carbon or phosphate by Escherichia coli K12: respective roles of acid glucose-1-phosphatase, hexose-phosphate permease, phosphoglucomutase and alkaline phosphatase
Metabolic role of the multiple forms of glucose-1-phosphatase, NAD+-and NADP+-dependent sorbitol dehydrogenases, acid phosphatase, and glucose-6-phosphate dehydrogenase in tissues and organs of the silkworm