Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera

Goudru, H G and Kumar, Sathish and Jayalakshmi, S K and Ballal, C R and Sharma, H C and Sreeramulu, K (2013) Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera. Entomological Research, 43 (1). pp. 55-62. ISSN 1748-5967

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Abstract

Phenoloxidases are oxidative enzymes, which play an important role in both cell mediated and humoral immunity. Purification and biochemical characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera (Hübner) were carried out to study its biochemical properties. Prophenoloxidase consists of a single polypeptide chain with a relative molecular weight of 85 kDa as determined by SDS–PAGE, MALDI–TOF MS and LC–ESI MS. After the final step, the enzyme showed 71.7 fold of purification with a recovery of 49.2%. Purified prophenoloxidase showed high specific activity and homology with phenoloxidase subunit-1 of Bombyx mori and the conserved regions of copper binding (B) site of phenoloxidase. Purified prophenoloxidase has pH optima of 6.8 and has high catalytic efficiency towards the dopamine as a substrate in comparison to catechol and L-Dopa. The PO activity was strongly inhibited by phenylthiourea, thiourea, dithiothreitol and kojic acid.

Item Type: Article
Divisions: UNSPECIFIED
CRP: UNSPECIFIED
Uncontrolled Keywords: copper binding B site; Helicoverpa armigera; Kojic acid; prophenoloxidase
Subjects: Others > Entomology
Depositing User: Mr Sanat Kumar Behera
Date Deposited: 24 Jan 2013 11:30
Last Modified: 17 Oct 2017 04:13
URI: http://oar.icrisat.org/id/eprint/6464
Official URL: http://dx.doi.org/10.1111/1748-5967.12002
Projects: University Grant Commission under Special Assistance Program(UGC-SAP)
Funders: Government of India - Department of Science and Technology, Government of India- University Grant Commission
Acknowledgement: We are thankful to University Grant Commission (UGC) for providing the fellowship under UGC-RFSMS scheme during this work. This research was supported by a research grant from the Department of Science and Technology (DST), New Delhi, to K. Sreeramulu and University Grant Commission under Special Assistance Program (UGCSAP), New Delhi, India. We also thank the Director Rabindra R. J and Dr. Jalali, S. K., Principal Scientist, NBAII, Bangalore, India, for providing the lab facilities throughout this work
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