Ovádi J, Salerno C, Keleti T, Fasella P
Eur J Biochem. 1978 Oct 16;90(3):499-503. doi: 10.1111/j.1432-1033.1978.tb12629.x.
Polarization of fluorescence measurements of aldolase and D-glyceraldehyde-3-phosphate dehydrogenase labeled with fluorescein isothiocyanate have been used to detect the possible formation of a soluble complex between the proteins. The results suggest an interaction between aldolase and D-glyceraldehyde-3-phosphate dehydrogenase with an apparent dissociation constant 3 X 10(-7) M and an apparent stoichiometry of two aldolase tetramers bound per tetramer of D-glyceraldehyde-3-phosphate dehydrogenase.
用异硫氰酸荧光素标记的醛缩酶和3-磷酸甘油醛脱氢酶的荧光偏振测量法已用于检测蛋白质间可能形成的可溶性复合物。结果表明醛缩酶与3-磷酸甘油醛脱氢酶之间存在相互作用，其表观解离常数为3×10⁻⁷M，且每分子3-磷酸甘油醛脱氢酶四聚体结合两分子醛缩酶四聚体的表观化学计量比。
