Pochon F, Favaudon V, Bieth J
Biochem Biophys Res Commun. 1983 Mar 29;111(3):964-9. doi: 10.1016/0006-291x(83)91394-3.
Free thiol groups released on proteolytic attack of alpha 2-macroglobulin by trypsin or chymotrypsin bind covalently to thiopropyl-Sepharose, indicating that they are located at the surface of the complexes. These cysteine sulfhydryl groups appear to be in contact with the alpha 2M-bound proteases from singlet-singlet energy transfer measurements between fluorescein isothiocyanate-labeled proteinases and N-(iodoacetylaminoethyl)-5-naphtylamine-1-sulfonic acid-labeled thiols in alpha 2-macroglobulin.
通过胰蛋白酶或糜蛋白酶对α2-巨球蛋白进行蛋白水解攻击所释放的游离巯基会与硫丙基琼脂糖共价结合，这表明它们位于复合物的表面。根据异硫氰酸荧光素标记的蛋白酶与α2-巨球蛋白中N-（碘乙酰氨基乙基）-5-萘胺-1-磺酸标记的巯基之间的单重态-单重态能量转移测量结果，这些半胱氨酸巯基似乎与α2M结合的蛋白酶接触。
