Kettner C, Springhorn S, Shaw E
Hoppe Seylers Z Physiol Chem. 1978 Sep;359(9):1183-91. doi: 10.1515/bchm2.1978.359.2.1183.
A survey of the reactivity of 16 peptidyl-argininyl-chloromethanes with boar acrosin indicated that these compounds as a general group of reagents were highly effective in the inactivation of acrosin since at least half of the reagents tested rapidly inactivated this protease at a concentration of 0.10 micrometer or lower. For example, Dns-Glu-Gly-ArgCH2Cl inactivates acrosin by 50% in 1.8 min at a concentration of 75 nM, whereas in contrast, a 14000-fold higher concentration of Nalpha-tosyllysyl-chloromethane is required to obtain an equivalent rate of inactivation. A comparison of the reactivity of acrosin and trypsin with the peptides of arginyl-chloromethane containing different substituents in the P2 and P3 positions suggests that the secondary binding sites of these two proteases are very similar. Reagents with homoarginine, lysine and D-arginine in the P1 position have also been prepared and evaluated, but these were considerably less effective than the corresponding arginyl-chloromethanes in the inactivation of both acrosin and trypsin.
一项对16种肽基 - 精氨酰 - 氯甲烷与猪顶体蛋白酶反应活性的研究表明，作为一类试剂，这些化合物在使顶体蛋白酶失活方面非常有效，因为至少一半测试的试剂在浓度为0.10微摩尔或更低时能迅速使这种蛋白酶失活。例如，Dns - Glu - Gly - ArgCH2Cl在浓度为75 nM时，1.8分钟内可使顶体蛋白酶失活50%，而相比之下，需要高14000倍浓度的Nα - 甲苯磺酰赖氨酰 - 氯甲烷才能获得同等的失活速率。对顶体蛋白酶和胰蛋白酶与在P2和P3位置含有不同取代基的精氨酰 - 氯甲烷肽段的反应活性比较表明，这两种蛋白酶的二级结合位点非常相似。还制备并评估了在P1位置含有高精氨酸、赖氨酸和D - 精氨酸的试剂，但这些试剂在使顶体蛋白酶和胰蛋白酶失活方面远不如相应的精氨酰 - 氯甲烷有效。
