phosphorylase activity is induced during ripening and is associated with the onset of starch degradation. Regulation is mainly dependent on gene expression, and the absence of ethylene perception by 1-methylcyclopropane has a positive effect
the enzyme is a target for development of inhibitors to prevent unwanted hepatic glycogenolysis under high glucose conditions in treatment of diabetes type 2 in humans
a highly sensitive and convenient assay for glycogen phosphorylase activity by analysing its chainlengthening action on a fluorogenic maltooligosaccharide derivative in a glucose-1-phosphate-rich medium. A maltotetraosyl residue comprising the non-reducing-end of a pyridylaminated maltooligosaccharide is indispensable for the chain-lengthening action of phosphorylase, and pyridylaminated maltohexaose is the most suitable substrate. Pyridylaminated maltoheptaose produced by the chain elongation reaction can be isolated and quantified at 10 fmol. Method has about 1000 times greater sensitivity than the spectrophotometric phosphate assay
study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation. Test system for the study of the effects of macromolecular crowding induced by osmolytes on aggregation of proteins
pentacyclic triterpenes, as inhibitors of glycogen phosphorylase, hold promise for the treatment of type-2 diabetes and other diseases with disorders in glycogen metabolism
the enzyme glycogen phosphorylase constitutes an adequate pharmacological target to modulate cellular glycogen levels, by means of inhibition of its catalytic activity
the enzyme is an important target for is a validated target for the development of type 2 diabetes treatments and the discovery of hypoglycaemic agents, both synthetic and natural
the enzyme is an important target for is a validated target for the development of type 2 diabetes treatments and the discovery of hypoglycaemic agents, both synthetic and natural
the enzyme is an important target for is a validated target for the development of type 2 diabetes treatments and the discovery of hypoglycaemic agents, both synthetic and natural
presubiculum, but not subiculum, of entorhinal cortex, is strongly reactive for glycogen phosphorylase. Glycogenolytic demand in Layers I and II is organized in a modular fashion and demand can be modified by brief exposure of animals to a novel holeboard
use of commercially available glycogen phosphorylase BB ELISA assay for diagnosis of myocardial damage and comparison with established cardiac markers such as troponin T, creatine kinase isoenzyme MB mass, and myoglobin. Glycogen phosphorylase BB is a promising marker for the early diagnosis of acute coronary syndrome and could probably act as a marker of ischemia
inhibition of the liver glycogen targeting subunit/glycogen phosphorylase interaction may provide an attractive approach for rebalancing the disturbed glycogen metabolism in diabetic patients (prevention of the GLGP interaction increases the glycogen synthesis rate)
production of D-glucose-1-phosphate with yield of 47% w/w from a reaction containing 5% w/v soluble starch in 0.7 M potassium phosphate. Purification of D-glucose-1-phosphate by ethanol preciptitation
maltodextrin phosphorylase from Pyrococcus furiosus is fused with the cellulose-binding domain of Clostridium cellulovorans serving as an aggregation module. After molecular cloning of the corresponding gene fusion construct and controlled expression in Escherichia coli BL21, 83% of total maltodextrin phosphorylase activity is displayed in active inclusion bodies. These active inclusion bodies are easily isolated by nonionic detergent treatment and directly used for maltodextrin conversion to alpha-D-glucose-1-phosphate in a repetitive batch mode. Only 10% of enzyme activity is lost after ten conversion cycles at optimum conditions
immobilization of partially purified enzyme using egg shell as solid support with a percentage retention of the enzyme on egg shell of nearly 56%. After immobilization, specific activity of the enzyme increases from 0. 0225 to 0.0452 with a concomitant slight alkaline shift in the optimum pH when assayed in both the directions. The immobilized enzyme also displays increased optimum temperature and thermo-stability and can be reused number of times. Use of immobilized enzyme for the production of glucose-1-phosphate
production of D-glucose-1-phosphate with yield of 47% w/w from a reaction containing 5% w/v soluble starch in 0.7 M potassium phosphate. Purification of D-glucose-1-phosphate by ethanol preciptitation