Caccuri A M, Aceto A, Rosato N, Di Ilio C, Piemonte F, Federici G
Dipartimento di Biologia, Università Tor Vergata, Roma.
Ital J Biochem. 1991 Sep-Oct;40(5):304-11.
The binding of the GSH to the GSH transferase pi quenches the protein intrinsic fluorescence more than the binding of GS-Me. The calculated dissociation constants are 38.6 microM and 90.9 microM for GSH and GS-Me, respectively. From the reported data it is evident that the binding of GSH to GSH transferase pi quenches the intrinsic fluorescence with two different mechanisms. The first one is a conformational change induced by the binding of the GSH and it is present also with the GS-Me binding. A second proposed mechanism is a contact quenching between the sulphydryl GSH group and a tryptophan residue. This suggests that at least one of the tryptophan residues is located near the GSH binding site.
谷胱甘肽（GSH）与谷胱甘肽转移酶π的结合比GS-甲基（GS-Me）的结合更能淬灭蛋白质的固有荧光。GSH和GS-Me的计算解离常数分别为38.6微摩尔和90.9微摩尔。从报告的数据可以明显看出，GSH与谷胱甘肽转移酶π的结合通过两种不同的机制淬灭固有荧光。第一种是由GSH结合诱导的构象变化，GS-Me结合时也存在这种变化。提出的第二种机制是巯基GSH基团与色氨酸残基之间的接触淬灭。这表明至少有一个色氨酸残基位于GSH结合位点附近。
