Hoshino N, Nakajima R, Yamazaki I
Iatron Laboratories Inc., Tokyo.
J Biochem. 1987 Oct;102(4):785-91. doi: 10.1093/oxfordjournals.jbchem.a122116.
The phenol oxidation catalyzed by horseradish peroxidase (HRP) is slowed down by the presence of excess H2O2. This inhibition is due to accumulation of Compound III, which is a catalytically sluggish form of HRP. When HRP is polymerized through covalent bonds, Compound III becomes unstable and the peroxidase activity is less sensitive to excess H2O2. Under suitable experimental conditions, the phenol oxidation is increased by about 20-fold upon polymerization of the enzyme. This fact represents the principle of a homogeneous enzyme immunoassay reported by Hoshino et al. (J. Biochem. 97, 113-118 (1985)). The ratio of the peroxidase activities of monomeric and polymerized HRPs is 1 : 4 when phenol is replaced by resorcinol, and the difference is no larger when guaiacol and catechol are used as electron donors.
辣根过氧化物酶（HRP）催化的苯酚氧化反应会因过量过氧化氢的存在而减慢。这种抑制作用是由于化合物III的积累，它是HRP的一种催化活性较低的形式。当HRP通过共价键聚合时，化合物III变得不稳定，过氧化物酶活性对过量过氧化氢的敏感性降低。在合适的实验条件下，酶聚合后苯酚氧化反应增加约20倍。这一事实代表了Hoshino等人报道的均相酶免疫测定原理（《生物化学杂志》97卷，113 - 118页（1985年））。当用间苯二酚代替苯酚时，单体和聚合HRP的过氧化物酶活性之比为1 : 4，当使用愈创木酚和儿茶酚作为电子供体时，差异也不大。
