McKenzie H A, White F H
Biochem Int. 1987 Feb;14(2):347-56.
alpha-Lactalbumin (alpha-LA) has been examined with a new and sensitive method for determination of lysozyme activity. Samples of bovine, human, equine, and rat alpha-LA exhibited cell lytic activity, from 2 X 10(-6) to 45 X 10(-6) of the specific activity of hen eggwhite lysozyme. The activity was chromatographically inseparable from bovine and human alpha-LA. Bovine serum albumin and purified beta-lactoglobulin were inactive. The pH profiles and reaction kinetics of bovine and human alpha-LA showed differences from those of the corresponding milk lysozymes, indicating that their lytic activities were not likely to have resulted from trace lysozyme content. Thus, it appears that a weak cell lytic activity is inherent to alpha-LA.
已采用一种测定溶菌酶活性的新型灵敏方法对α-乳白蛋白（α-LA）进行了检测。牛、人、马和大鼠α-LA样品均表现出细胞裂解活性，其活性为鸡蛋清溶菌酶比活性的2×10⁻⁶至45×10⁻⁶。该活性通过色谱法无法与牛和人α-LA分离。牛血清白蛋白和纯化的β-乳球蛋白无活性。牛和人α-LA的pH曲线及反应动力学与相应的乳溶菌酶不同，这表明它们的裂解活性不太可能是由痕量溶菌酶含量导致的。因此，看来α-LA本身具有较弱的细胞裂解活性。
