Document Detail

Characterization and ecological implications of midgut proteolytic activity in larvalPieris rapae andTrichoplusia ni.
MedLine Citation:
PMID:  24272299     Owner:  NLM     Status:  In-Data-Review    
In their larval luminal midgut fluid,Trichoplusia ni (Lepidoptera: Noctuidae) andPieris rapae (Lepidoptera: Pieridae) contain endopeptidases as their primary proteases. Neither species has detectable exopeptidase activity. Studies using enzyme-specific substrates and inhibitors demonstrate that the endopeptidases are serine proteinases (both trypsinlike and chymotrypsinlike) with histidine at the active site. Optimal pH for the tryptic and chymotryptic activity is 8.5 and 8.0, respectively, forT. ni. and 8.0 and 9.0, respectively, forP. rapae. The efficiency of proteolytic digestion (as measured by the rate of in vitro digestion of a standard protein by the midgut luminal fluid) is positively correlated with the larval dietary protein requirement and is significantly influenced by the ratios of tryptic to chymotryptic activity present in the gut lumen of these two species of Lepidoptera.
R M Broadway
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of chemical ecology     Volume:  15     ISSN:  0098-0331     ISO Abbreviation:  J. Chem. Ecol.     Publication Date:  1989 Jul 
Date Detail:
Created Date:  2013-11-25     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7505563     Medline TA:  J Chem Ecol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2101-13     Citation Subset:  -    
Department of Entomology New York State Agricultural Experiment Station, Cornell University, 14456, Geneva, New York.
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