Carlsson J
Biochem Biophys Res Commun. 1983 Oct 31;116(2):568-73. doi: 10.1016/0006-291x(83)90561-2.
Lactoperoxidase catalyzed the catalatic decomposition of H2O2 in the presence of SCN-. The pH optimum for O2 evolution was 8.5, while the enzyme activity as disclosed by the rate of H2O2 disappearance was optimal at 4.5. Since the catalatic activity of lactoperoxidase was SCN- dependent, and no O2 was evolved, when H2O2 was added to OSCN- in the absence of lactoperoxidase, an enzyme-OSCN complex may be assumed to be an intermediate in the catalatic activity of lactoperoxidase.
在硫氰酸盐（SCN-）存在的情况下，乳过氧化物酶催化过氧化氢（H2O2）的催化分解。氧气释放的最适pH值为8.5，而过氧化氢消失速率所显示的酶活性在pH 4.5时最佳。由于乳过氧化物酶的催化活性依赖于硫氰酸盐，并且在没有乳过氧化物酶的情况下向硫氰酸（OSCN-）中加入过氧化氢时不会释放氧气，因此可以假定酶-硫氰酸复合物是乳过氧化物酶催化活性的中间产物。
