Wikstrom P, Anagli J, Angliker H, Shaw E
Friedrich Miescher-Institut, Basel, Switzerland.
J Enzyme Inhib. 1992;6(4):259-69. doi: 10.3109/14756369309020176.
Calpain, the calcium-activated cysteinyl proteinase, can be irreversibly inactivated by peptidyl diazomethyl ketones in which the peptide portion contains a penultimate leucine residue. Some new derivatives of this type have been synthesized and examined for their rates of inactivation of chicken gizzard and human platelet calpain. Two derivatives containing a C-terminal biotin residue, Biot-Aca-Leu-TyrCHN2 and Biot-Aca-Leu-Leu-TyrCHN2, have also been prepared in the expectation that their application to the study of the function of calpain and related proteases will prove fruitful.
钙蛋白酶，即钙激活半胱氨酸蛋白酶，可被肽基重氮甲基酮不可逆地失活，其中肽部分含有倒数第二个亮氨酸残基。已合成了这类的一些新衍生物，并检测了它们对鸡砂囊和人血小板钙蛋白酶的失活速率。还制备了两种含有C端生物素残基的衍生物，即生物素-Aca-Leu-TyrCHN2和生物素-Aca-Leu-Leu-TyrCHN2，期望它们在钙蛋白酶及相关蛋白酶功能研究中的应用将卓有成效。
