Document Detail

Bio-potency of a 21 kDa Kunitz-type trypsin inhibitor from Tamarindus indica seeds on the developmental physiology of H. armigera.
MedLine Citation:
PMID:  25454525     Owner:  NLM     Status:  Publisher    
A trypsin inhibitor purified from the seeds of Tamarindus indica by Sephadex G-75, DEAE-Sepharose and Trypsin-Sepharose CL-4B columns was studied for its antifeedant, larvicidal, pupicidal and growth inhibitory activities against Helicoverpa armigera larvae. Tamarindus trypsin inhibitor (TTI) exhibited inhibitory activity towards total gut proteolytic enzymes of H. armigera (~87%) and bovine trypsin (~84%). Lethal doses which caused mortality and weight reduction by 50% were 1% w/w and 0.50% w/w, respectively. IC50 of TTI against Helicoverpa midgut proteases and bovine trypsin were ~2.10 µg/ml and 1.68 µg/ml respectively. In larval feeding studies the 21 kDa Kunitz-type protein was found to retard growth and development, prolonged the larval-pupal development durations along with adversely affecting the fertility and fecundity of H. armigera. In artificial diet at 0.5% w/w TTI, the efficiency of conversion of ingested food as well as of digested food, relative growth rate, growth index declined whereas approximate digestibility, metabolic cost, relative consumption rate, consumption index and total developmental period enhanced for H. armigera larvae. These results suggest that TTI has toxic and adverse effect on the developmental physiology of H. armigera and could be useful in controlling the pest H. armigera.
Prabhash K Pandey; Farrukh Jamal
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-10-13
Journal Detail:
Title:  Pesticide biochemistry and physiology     Volume:  116C     ISSN:  1095-9939     ISO Abbreviation:  Pestic Biochem Physiol     Publication Date:  2014 Nov 
Date Detail:
Created Date:  2014-12-2     Completed Date:  -     Revised Date:  2014-12-3    
Medline Journal Info:
Nlm Unique ID:  1301573     Medline TA:  Pestic Biochem Physiol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  94-102     Citation Subset:  -    
Copyright Information:
Copyright © 2014 Elsevier Inc. All rights reserved.
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