Yip B P, Rudolph F B
J Biol Chem. 1977 Mar 25;252(6):1844-6.
Reacting enzyme sedimentation studies have been performed with yeast hexokinase isozymes A and B in the presence and absence of chromium ATP at pH 6.75. Preincubation of either isozyme with CrATP causes a shift in the monomer-dimer equilibrium toward the monomeric form. The results are consistent with the observed increase in inhibition caused by CrATP (Danenberg, K.D., and Cleland, W.W. (1975) Biochemistry 14, 28-39) being due to a conformational change in the protein which causes a decrease in the association constant for the monomer.
在pH 6.75条件下,在有和没有铬ATP存在的情况下,对酵母己糖激酶同工酶A和B进行了反应酶沉降研究。任何一种同工酶与CrATP预孵育都会导致单体-二聚体平衡向单体形式转变。这些结果与观察到的CrATP引起的抑制作用增加(Danenberg,K.D.和Cleland,W.W.(1975年)《生物化学》14,28 - 39)一致,这是由于蛋白质的构象变化导致单体的缔合常数降低。