Nadirashvili N Sh, Simonidze M Sh
Biofizika. 1982 Jul-Aug;27(4):584-6.
It has been established that the molecule of alpha-actinin (m. w. 200 000) contains 16 SH-groups, which are distinguished by their activity. Six SH-groups may be comparatively easily discovered in the native protein. Four partly "masked" SH-groups are titrated in the low acidic media. Five-six SH-groups are completely masked and are revealed only after denaturation of protein. Blocking of SH-groups of alpha-actinin by the parachloromercuribenzoate decreases the biological activity of alpha-actinin measured by the formation of the alpha-actinin--actin complex. It has been shown that partly "masked" SH-groups revealed with the temperature increase are not incorporated into the active centre and do not take part in protein functioning.
已经确定，α-辅肌动蛋白分子（分子量200 000）含有16个巯基，这些巯基因其活性而有所不同。在天然蛋白质中，六个巯基相对容易被发现。四个部分“被掩盖”的巯基在低酸性介质中被滴定。五到六个巯基被完全掩盖，只有在蛋白质变性后才会显现出来。对氯汞苯甲酸对α-辅肌动蛋白巯基的封闭会降低通过α-辅肌动蛋白-肌动蛋白复合物形成来测定的α-辅肌动蛋白的生物活性。已经表明，随着温度升高而显现的部分“被掩盖”的巯基不会纳入活性中心，也不参与蛋白质的功能。
