Binding of muscle phosphorylase B by glycogen
Chebotareva, N.A.; Lisovskaia, N.P.; Kurganov, B.I.
Molekuliarnaia Biologiia 13(1): 228-236
1979
ISSN/ISBN: 0026-8984 PMID: 460193 Document Number: 146601
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.