EC Number |
Application |
Reference |
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2.4.1.1 | agriculture |
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 |
674124 |
2.4.1.1 | analysis |
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 |
704360 |
2.4.1.1 | analysis |
use of phosphorylase and tissue ATPase as biomarkers for exposure of aquatic organisms to cypermethrin intoxication |
706837 |
2.4.1.1 | biotechnology |
enzyme is a useful marker in the regulation of of glycogen metabolism and reproduction of Crassostrea gigas |
658478 |
2.4.1.1 | biotechnology |
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 |
672290 |
2.4.1.1 | drug development |
glycogen phosphorylase is an active target of research in search of inhibitors for the treatment of type II diabetes |
718873 |
2.4.1.1 | drug development |
pentacyclic triterpenes, as inhibitors of glycogen phosphorylase, hold promise for the treatment of type-2 diabetes and other diseases with disorders in glycogen metabolism |
719407 |
2.4.1.1 | drug development |
the enzyme glycogen phosphorylase constitutes an adequate pharmacological target to modulate cellular glycogen levels, by means of inhibition of its catalytic activity |
736933 |
2.4.1.1 | drug development |
the enzyme is a target for inhibitor design in development of drugs for treatment of type 2 diabetes |
719047 |
2.4.1.1 | drug development |
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 |
-, 735773 |