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糖原磷酸化酶（Glycogen phosphorylase，GP，EC 2.4.1.1)）是糖原分解代谢的关键酶，使糖原分子从非还原端逐个断开α-1，4-糖苷键移去葡萄糖基，释放1-磷酸葡萄糖，直至临近糖原分子α-1，6-糖苷键分支点前4个葡萄糖基处。GP分为有活性的糖原磷酸化酶a（GPa）和无活性的糖原磷酸化酶b（GPb）两种形式。GPb在一定浓度的腺苷酸（5，-AMP）存在下可被激活。 测定原理：GP催化糖原和无机磷产生葡萄糖残基生成糖原和1-磷酸葡萄糖，磷酸葡萄糖变位酶和6-磷酸葡萄糖脱氢酶进一步依次催化NADP还原生成NADPH，在340nm下测定NADPH上升速率，即可反映GP活性。添加一定浓度的腺苷酸（5，-AMP）时测定GP（GPa和GPb）活性，未添加腺苷酸（5，-AMP）时测定GPa活性，GP活性－GPa活性得到GPb活性。
Glycogen phosphorylase (GP, EC 2.4.1.1) is a key enzyme in glycogen catabolism. It cleaves α-1,4-glycosidic bonds one by one from the non-reducing ends of the glycogen molecule, removing glucosyl residues and releasing glucose-1-phosphate, until it reaches four glucose residues before the α-1,6-glycosidic branch points. GP exists in two forms: the active glycogen phosphorylase a (GPa) and the inactive glycogen phosphorylase b (GPb). GPb can be activated in the presence of a certain concentration of adenylate (5'-AMP). Determination Principle: GP catalyzes the reaction between glycogen and inorganic phosphate, producing a shortened glycogen molecule and glucose-1-phosphate. Phosphoglucomutase and glucose-6-phosphate dehydrogenase subsequently catalyze the reduction of NADP⁺ to NADPH. GP activity is determined by measuring the rate of increase in NADPH at 340 nm. GP (GPa and GPb) activity is measured in the presence of a certain concentration of adenylate (5'-AMP), while GPa activity is measured in the absence of adenylate (5'-AMP). GPb activity is obtained by subtracting GPa activity from total GP activity.
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