Yamada H, Takamori K, Ogawa H
Arch Dermatol Res. 1987;279(3):194-7. doi: 10.1007/BF00413257.
Skin sulfhydryl oxidase (SSO) was prepared from cow snout skin. Dithiothreitol was the thiol substrate most efficiently utilized, with 2-mercaptoethanol, glutathione, and cysteine having less than 23% the relative efficiency of dithiothreitol. In the presence of SSO reductively denatured ribonuclease A was reoxidized and reactivated. The degree of reactivation was proportional to the incubation time and dependent on the amount of enzyme added. The oxidation of thiols by SSO required molecular oxygen as an oxidant. The oxygen consumption increased linearly with the increasing concentration of SSO during the increasing formation of disulfide from sulfhydryl groups. The activity of SSO was detected in differing amounts in each of the four layers--stratum corneum, stratum granulosum, stratum spinosum with basal cell layer, and dermis--of cow snout skin, while showing the highest specific activity in the stratum granulosum.
皮肤巯基氧化酶（SSO）是从牛鼻皮肤中制备的。二硫苏糖醇是最有效地被利用的硫醇底物，2-巯基乙醇、谷胱甘肽和半胱氨酸的相对效率低于二硫苏糖醇的23%。在SSO存在的情况下，还原变性的核糖核酸酶A被重新氧化并重新激活。重新激活的程度与孵育时间成正比，并取决于所添加酶的量。SSO对硫醇的氧化需要分子氧作为氧化剂。在从巯基形成二硫键的过程中，耗氧量随着SSO浓度的增加而线性增加。在牛鼻皮肤的角质层、颗粒层、棘层与基底层以及真皮这四层中的每一层中都检测到了不同量的SSO活性，而在颗粒层中显示出最高的比活性。
