Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera

Goudru, Hanumanth G and Kumar, Sathish and Jayalakshmi, Senigala K and Ballal, Chandish R and Sharma, Hari C and Sreeramulu, Kuruba (2013) Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera. In: ENTOMOLOGICAL RESEARCH, 43 (1). pp. 55-62.

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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 (Hubner) 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 SDSPAGE, MALDITOF MS and LCESI 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:	Journal Article
Publication:	ENTOMOLOGICAL RESEARCH
Publisher:	WILEY-BLACKWELL
Additional Information:	Copyright for this article belongs to WILEY-BLACKWELL, USA
Keywords:	copper binding B site;Helicoverpa armigera; Kojic acid;prophenoloxidase
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	05 Mar 2013 06:15
Last Modified:	05 Mar 2013 06:15
URI:	http://eprints.iisc.ac.in/id/eprint/45955

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