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RISS 인기검색어
- 검색키워드
- 저자 : Chandish R. BALLAL (검색결과 2 건)
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Enakshi Ghosh,Chandish R. Ballal 한국응용곤충학회 2017 Journal of Asia-Pacific Entomology Vol.20 No.3
In Asia Corcyra cephalonica (Stainton) (Lepidoptera: Pyralidae) is widely used as a factitious host for the mass rearing of several bio-control agents viz. chrysopids, braconids, trichogrammatids and anthocorids. The age dependent cold storage amenability of C. cephalonica eggs was evaluated. At 5 ± 1 °C with a 24 h of scotophase, 0 to 22 h old eggs of C. cephalonica could be stored for up to 5 days resulting in 83 to 94% hatching. Eggs of C. cephalonica are UV irradiated for mass rearing of T. chilonis. Four, eight, sixteen and twenty four-hour-old C. cephalonica eggs were stored at 5 ± 1 °C for different durations prior to and post-UV irradiation and tested for their amenability to parasitism by T. chilonis. Adult females of T. chilonis could parasitise 67–78% of eggs stored for up to 10 days prior to UV treatment, while 74–78.2% parasitism was recorded in the case of eggs stored for 10 days post-UV. The host eggs of all age groups stored for 20 days (10 days pre-UV and 10 days post-UV) were effectively parasitised providing 83.8–88.4% parasitism. Eight and sixteen hour-old old host eggs stored for 30 days (15 days of pre-UV and 15 days of post-UV) recorded 70–80% parasitism. The host egg storage technique developed through this study would be beneficial for insectaries to stock the host eggs, which can lead to uninterrupted production and supply of ‘Tricho-cards’, especially during seasonal high demand.
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Purification and characterization of prophenoloxidase from cotton bollworm, Helicoverpa armigera
Hanumanth G. Goudru,Sathish KUMAR,Senigala K. JAYALAKSHMI,Chandish R. BALLAL,Hari C. SHARMA,Kuruba SREERAMULU 한국곤충학회 2013 Entomological Research Vol.43 No.1
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.
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