Klinov S V, Kurganov B I
A. N. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow.
Biochem Mol Biol Int. 1995 Mar;35(3):643-50.
The inhibition of glycogen phosphorylase b from rabbit skeletal muscles by the derivatives of riboflavin, FMN, FAD, and 2', 3', 4', 5'-tetraacetylriboflavin substituted in positions 6 and 8 of the isoalloxazine part of the flavin molecule is found to be cooperative (the Hill coefficient, h, exceeds 1.0). The modification of the flavin molecule slightly changes the value of the Hill coefficient, but results in the increase of the "half-saturation" concentration [I]0.5.
核黄素、黄素单核苷酸(FMN)、黄素腺嘌呤二核苷酸(FAD)以及在黄素分子异咯嗪部分6位和8位被取代的2', 3', 4', 5'-四乙酰核黄素对兔骨骼肌糖原磷酸化酶b的抑制作用具有协同性(希尔系数h超过1.0)。黄素分子的修饰略微改变了希尔系数的值,但导致“半饱和”浓度[I]0.5增加。