PEROXIDASE ACTIVITY OF HEMOPROTEINS .1. GENERATION OF ACTIVITY BY ACID OR ALKALI DENATURATION OF METHEMOGLOBIN AND CATALASE
PEROXIDASE ACTIVITY OF HEMOPROTEINS .1. GENERATION OF ACTIVITY BY ACID OR ALKALI DENATURATION OF METHEMOGLOBIN AND CATALASE
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DOI：
10.1016/0003-9861(61)90311-3
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发表时间：
1961-01-01
影响因子：
3.9
通讯作者：
KUROZUMI, T
中科院分区：
文献类型：
--
作者：
INADA, Y;SHIBATA, K;KUROZUMI, T
以无色孔雀石绿色（LMG）为供氢体，系统观察高铁血红蛋白和过氧化氢酶溶液的过氧化物酶活性对pH的依赖性，发现当这些血红蛋白被酸或碱变性时，会产生高活性。高铁血红蛋白的一半大小的亚基和过氧化氢酶的1/3大小的亚基形成的变性被认为是负责产生的活动。绝对速率常数，K1和K4，确定了过氧化物酶反应的高铁血红蛋白在最佳pH 4.8的半大小亚基。与LMG反应的速率常数k4值相当高，是中性溶液中天然分子值的500倍以上，尽管该值是辣根过氧化物酶k4值的四分之一。亚基和H2 O2之间的反应的k1值远小于常见的过氧化物酶的k1值，并且大约是亚基的k4值的百分之一。
The systematic observation of the pH dependencies of the peroxidase activities of methemoglobin and catalase solutions with leucomalachite green(LMG) as the hydrogen donor revealed the fact that a high activity is generated when these hemoproteins are denatured by acid or alkali. The half-size subunit of methemoglobin and the 1/3 size subunit of catalase formed by the denaturation were found to be responsible for the activities generated. Absolute rate constants, k1 and k4, were determined for the peroxidase reaction by the half-size subunit of methemoglobin at the optimum pH 4.8. The k4 value which is the rate constant for the reaction with LMG was quite high and more than 500 times the value for the native molecule in the neutral solution, although the value was one-quarter the k4 value for horse-radish peroxidase. The k1 value for the reaction between the subunit and H2O2 was much smaller than the k1 values for common peroxidases, and was approximately one-hundredth the k4 value for the subunit.