Villalobo A, Harris J W, Roufogalis B D
Biochim Biophys Acta. 1986 Jun 13;858(1):188-94. doi: 10.1016/0005-2736(86)90305-6.
The ATP hydrolytic activity of the solubilized and purified Ca2+-translocating ATPase from human erythrocyte plasma membrane was strongly inhibited by the nonpolar compound, N,N'-dicyclohexylcarbodiimide, both in the presence and in the absence of calmodulin. However, the more water-soluble carbodiimides, 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide and 1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide had little inhibitory effect on the enzyme. The inhibitory effect of N,N'-dicyclohexylcarbodiimide was most pronounced at acid pH, and declined sharply at alkaline pH values. In addition, the optimum pH for the enzyme activity also shifted to more alkaline values in the presence of the carbodiimide. Calcium ion appears to favor the inhibition induced by the carbodiimide, in contrast to the observed protection by Ca2+ in the sarcoplasmic reticulum Ca2+-translocating ATPase. N,N'-Dicyclohexylcarbodiimide also dramatically decreased the stimulatory effect of calmodulin on the activity of the enzyme.
在有和没有钙调蛋白的情况下，人红细胞质膜中溶解并纯化的Ca2+转运ATP酶的ATP水解活性均受到非极性化合物N，N'-二环己基碳二亚胺的强烈抑制。然而，水溶性更强的碳二亚胺，1-乙基-3-（3-二甲基氨基丙基）碳二亚胺和1-环己基-3-（2-吗啉代乙基）碳二亚胺对该酶的抑制作用很小。N，N'-二环己基碳二亚胺的抑制作用在酸性pH下最为明显，而在碱性pH值下急剧下降。此外，在存在碳二亚胺的情况下，酶活性的最适pH值也向更碱性的值移动。与在肌浆网Ca2+转运ATP酶中观察到的Ca2+保护作用相反，钙离子似乎有利于碳二亚胺诱导的抑制作用。N，N'-二环己基碳二亚胺还显著降低了钙调蛋白对该酶活性的刺激作用。
