[Binding of muscle phosphorylase B by glycogen].
The binding of phosphorylase B with glycogen has been studied by means of analytical ultracentrifuge with absorption optics and a photoelectric scanner. Adsorbtion capacity for pig liver glycogen with respect to phosphorylase B (aM) and microscopic dissociation constant of enzyme -- glycogen complex (K) have been determined (aM = 3.64 . 10(-6) moles of bound enzyme per 1 g of glycogen: K = 2.6 . 10(-7) M at 12.7 degrees, pH 6.8). For oyster glycogen the value of aM is equal to 3.92 . 10(-6) moles of the bound protein per 1g of glycogen and K = 6.8 . 10(-7) M. The method of determination of microscopic Michaelis constant with respect to glycogen using known value of aM has been demonstrated.
D000818:Animals; D006003:Glycogen; D007700:Kinetics; D008112:Liver Glycogen; D008433:Mathematics; D009132:Muscles / Q000201:enzymology; D010125:Ostreidae; D010763:Phosphorylase b / Q000378:metabolism*; D006005:Phosphorylases / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D013552:Swine
D008112:Liver Glycogen; D006003:Glycogen; D010763:Phosphorylase b; D006005:Phosphorylases
Izuchenie sviazyvaniia myshechnoĭ fosforilazy b glikogenom.