Saint-Blancard J, Allary M, Hartmann S, Caquet D, Berthou J, Jollès P
Biochimie. 1975;57(10):1163-6. doi: 10.1016/s0300-9084(76)80578-0.
The influence of urea and of guanidine chloride on the binding of the bacterial substrate and of inhibitors such as N-acetylglucosamine or chitotetraose to hen lysozyme were studied at 20 degrees and at 40 degrees C (physiological temperature). The action of urea did not prevent a certain degree of organization of the enzyme compatible with its usual behaviour in the presence of some inhibitors and with its crystallization ; guanidine chloride, already at low concentrations, seemed to have a more severe effect on lysozyme.
研究了尿素和氯化胍在20℃和40℃（生理温度）下对细菌底物以及诸如N-乙酰葡糖胺或壳四糖等抑制剂与母鸡溶菌酶结合的影响。尿素的作用并未阻止酶形成一定程度的结构，这种结构与它在某些抑制剂存在时的通常行为及其结晶情况相符；而氯化胍，即使在低浓度下，似乎对溶菌酶有更严重的影响。
