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Title: [Glycogen phosphorylase from human leukocytes. Isolation and kinetic properties]. Author: Lebedeva OV, Frumkina IG, Ugarova NN, Cherniad'eva IF, Ameliushkina VA, Titov VN. Journal: Biokhimiia; 1990 Jan; 55(1):65-72. PubMed ID: 2111714. Abstract: Homogeneous glycogen phosphorylase from human leukocytes has been obtained. A one-step bioluminescent procedure for the enzyme activity assay has been developed. This method is based on a continuous recording of the product of the glycogen phosphorylase-catalyzed reaction using a coimmobilized multienzyme system (phosphoglucomutase, glucose-6-phosphate dehydrogenase, NADH:FMN oxidoreductase and bacterial luciferase). The method sensitivity is 10 times as high compared to earlier described methods. The Km values for glycogen (0.2 mg/ml) and phosphate (3.9 mM) at pH 7.9 were determined. AMP was shown to be the enzyme effector.[Abstract] [Full Text] [Related] [New Search]