Purification and characterization of prophenoloxidase from Galleria mellonella L.

Dudu Demir, Nahit Gençer, Aylin Er
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引用次数: 23

Abstract

Prophenoloxidase (PPO) was purified from Galleria mellonella L. A 67-fold purification of the proenzyme with 352% yield was achieved by using a Sepharose 4B-L-tyrosine-p-amino benzoic acid affinity column. The purified enzyme was migrated as a single band on SDS-polyacrylamide gel electrophoresis. K(m) and V(max) values were 0.017 M and 1430.45 EU for catechol. Inhibition of PPO was investigated with inhibitors such as p-aminobenzoic acid, etyleneglycol, and ascorbic acid. Among them, ascorbic acid showed the strongest inhibitory activity with IC(50) value of 2.94 μM. The current paper represents new strategies for the biological control of the Galleria mellonella L. insect.

mellonella原酚氧化酶的纯化及特性研究。
采用Sepharose 4b - l -酪氨酸-对氨基苯甲酸亲和柱纯化,得到67倍纯化,产率为352%。纯化后的酶在sds -聚丙烯酰胺凝胶电泳上呈单条带迁移。儿茶酚的K(m)和V(max)分别为0.017 m和1430.45 EU。研究了对氨基苯甲酸、乙二醇和抗坏血酸等抑制剂对PPO的抑制作用。其中抗坏血酸的抑制活性最强,IC(50)值为2.94 μM。本文提出了一种新的生物防治策略。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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