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本文用等速电泳技术测定了25℃时LDS对肌酸激酶分子的饱和紧密结合数为87。Hill作图法和Scatchard作图法分析的结果表明,这种结合呈正协同效应。当LDS对酶的高亲和位点充分饱和时,酶完全丧失活力;但部分饱和时,酶的剩余活力却明显地大于被认为是游离酶所能提供的活力。这表明还存在着一些仅被LDS部分饱和的活性酶分子。ATP的存在会导致LDS对酶分子紧密结合的减少和酶活力的部分恢复。
In this paper, the saturation binding of LDS to creatine kinase at 25 ℃ was determined by means of isokinetic electrophoresis. The results of Hill mapping and Scatchard mapping show that this combination shows a positive synergistic effect. When LDS fully saturates the high affinity sites of the enzyme, the enzyme completely loses its vitality; however, when partially saturated, the remaining vitality of the enzyme is significantly greater than what is considered to be the activity of the free enzyme. This suggests that there are also active enzyme molecules that are only partially saturated with LDS. The presence of ATP results in a decrease of LDS binding to the enzyme molecule and a partial recovery of enzyme activity.