[Glycogen phosphorylase from human leukocytes. Isolation and kinetic properties].
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.
Lebedeva
O V
OV
Frumkina
I G
IG
Ugarova
N N
NN
Cherniad'eva
I F
IF
Ameliushkina
V A
VA
Titov
V N
VN
D000818:Animals; D002384:Catalysis; D006801:Humans; D007700:Kinetics; D007962:Leukocytes / Q000201:enzymology*; D009132:Muscles / Q000201:enzymology; D010762:Phosphorylase a / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism; D010763:Phosphorylase b / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism; D006005:Phosphorylases / Q000097:blood* / Q000302:isolation & purification / Q000378:metabolism; D011817:Rabbits; D013379:Substrate Specificity
D010762:Phosphorylase a; D010763:Phosphorylase b; D006005:Phosphorylases
Glikogenfosforilaza iz leĭkotsitov cheloveka. Vydelenie i kineticheskie svoĭstva.