Makale detayı · 2012
Purification and Characterization of Prophenoloxidase from Galleria mellonella L
Artificial Cells, Blood Substitutes and Biotechnology
- Yıl
- 2012
- ISSN
1073-1199- Tür
- article
Veri kaynağı ayrımı
- YÖKSİS YÖKSİS makale kaydı
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Özet
İngilizce (OpenAlex)
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.
Konular
- Invertebrate Immune Response Mechanisms
- Insect Utilization and Effects
- Neurobiology and Insect Physiology Research
Birincil konu Invertebrate Immune Response Mechanisms