Vasstrand E N, Jensen H B
Scand J Dent Res. 1980 Jun;88(3):219-28. doi: 10.1111/j.1600-0722.1980.tb01218.x.
Lysozyme from human saliva was purified in one step by affinity chromatography on chitin. The recovery, however, was always very low, typically 25-40%. When the cationic exchanger BioRex 70 was used, the enzyme was isolated from saliva with only minor loss of activity, and the product appeared to be 60-70% pure. This partially purified enzyme bound completely and reversibly to chitin and was thereby purified to homogeneity with little loss of activity (< 10%). Both saliva lysozyme and the chicken egg white lysozyme were found to exhibit their highest lytic activity at high pH/low ionic strength (pH 9.0, I = 0.03), and both enzymes required higher ionic strength) it was found, however, that the ratio of the specific activity of saliva lysozyme to that of chicken lysozyme varied considerably depending on the assay conditions used. We argue strongly, therefore, against the frequent use of chicken lysozyme as a standard of reference in work on human lysozyme.
通过几丁质亲和层析一步法纯化人唾液中的溶菌酶。然而，回收率一直很低，通常为25%-40%。当使用阳离子交换剂BioRex 70时，从唾液中分离出的酶活性仅有轻微损失，产物纯度似乎为60%-70%。这种部分纯化的酶能完全且可逆地结合到几丁质上，从而在活性损失很小（<10%）的情况下被纯化至同质。发现唾液溶菌酶和鸡蛋白溶菌酶在高pH/低离子强度（pH 9.0，I = 0.03）下均表现出最高的裂解活性，且两种酶都需要更高的离子强度。然而，发现唾液溶菌酶与鸡溶菌酶的比活性之比根据所使用的测定条件有很大差异。因此，我们强烈反对在人溶菌酶研究中频繁使用鸡溶菌酶作为参考标准。
