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Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera

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Relation http://oar.icrisat.org/6464/
http://dx.doi.org/10.1111/1748-5967.12002
 
Title Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera
 
Creator Goudru, H G
Kumar, Sathish
Jayalakshmi, S K
Ballal, C R
Sharma, H C
Sreeramulu, K
 
Subject Entomology
 
Description 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.
 
Publisher John Wiley & Sons, Inc. in association with the Entomological Society of Korea
 
Date 2013
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://oar.icrisat.org/6464/1/EntomologicalRes_43_55-62_2013.pdf
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