Rose M S
Biochem J. 1969 Jan;111(2):129-37. doi: 10.1042/bj1110129.
One molecule of rat haemoglobin binds two molecules of triethyltin. The binding sites are located on the globin and there is co-operativity between the sites such that the intrinsic affinity constant at pH8.0 increases from 3.5x10(5)m(-1) for the binding of the first triethyltin molecule to 5.0x10(5)m(-1) for the binding of the second. Evidence is presented, from pH studies and the kinetics of inhibition due to photo-oxidation, that each binding site contains two histidine residues.
一个大鼠血红蛋白分子能结合两个三乙基锡分子。结合位点位于珠蛋白上,且这些位点之间存在协同性,使得在pH8.0时,第一个三乙基锡分子结合的固有亲和常数为3.5×10⁵m⁻¹,而第二个三乙基锡分子结合的固有亲和常数增至5.0×10⁵m⁻¹。来自pH研究及光氧化所致抑制动力学的证据表明,每个结合位点含有两个组氨酸残基。