Peroxidase Isozymes from Horseradish Roots
Peroxidase Isozymes from Horseradish Roots
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DOI：
10.1016/s0021-9258(18)95985-5
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发表时间：
1967
期刊：
影响因子：
--
通讯作者：
E. Kay;L. Shannon;J. Y. Lew
中科院分区：
文献类型：
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作者：
E. Kay;L. Shannon;J. Y. Lew
本文报道了七种均相过氧化物酶同工酶的催化性质。在以邻二苯甲胺为底物的过氧化反应和以草酸乙酯为底物的氧化反应中，测定了各同工酶的催化性质。每种同工酶都能够催化两种底物的氧化，并且它们表现出相同的辅因子要求。除A-3同工酶在过氧化反应中迅速失活外，其余各同工酶的时间进程相同。同工酶A-1、A-2和A-3具有相似的催化性质，可归为一类。其余的同工酶B、C、D和E也具有相似的催化性质，可归为另一类。然而，两组同工酶在最适pH、比活力、表观Km值和对抑制剂的亲和力方面存在显著差异。
This report describes the catalytic properties of seven homogeneous peroxidase isozymes. The catalytic properties of each isozyme were determined in a peroxidatic reaction with the use ofo-dianisidine as the substrate, and in an oxidatic reaction with the use of oxalacetate as the substrate. Each isozyme was capable of catalyzing the oxidation of both substrates and they exhibited identical cofactor requirements. The time course for each isozyme was identical except for Isozyme A-3, which was inactivated rapidly in the peroxidatic reaction. Isozymes A-1, A-2, and A-3 possessed similar catalytic properties and were classified into one group. The remaining isozymes, B, C, D, and E, also possessed similar catalytic properties and were classified into another group. The two groups of isozymes, however, showed marked differences in pH optima, specific activities, apparentKmvalues, and affinity toward inhibitors.