{"title":"Purification and characterization of prophenoloxidase from Galleria mellonella L.","authors":"Dudu Demir, Nahit Gençer, Aylin Er","doi":"10.3109/10731199.2012.696060","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":8413,"journal":{"name":"Artificial cells, blood substitutes, and immobilization biotechnology","volume":"40 6","pages":"391-5"},"PeriodicalIF":0.0000,"publicationDate":"2012-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/10731199.2012.696060","citationCount":"23","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Artificial cells, blood substitutes, and immobilization biotechnology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3109/10731199.2012.696060","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2012/7/10 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
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.