Abstract:
:Two digestive trypsin-like proteinases from Sesamia nonagrioides Lef. (Lepidoptera: Noctuidae) larvae were purified by benzamidine-Sepharose affinity chromatography. The purified enzymes showed molecular size of 27 (trypsin-I) and 24 KDa (trypsin-II). Amino acid analysis and N-terminal sequencing confirmed their relationship with other trypsins from lepidopteran larvae. However, trypsin-I presented one lysine at position 11, being the first report of this amino acid in the sequence of a lepidopteran digestive trypsin. Trypsin-I had an isoelectric point of 6.0, and a Km of 2.2 x 10(-4) M and 3.9 x 10(-5) M for BApNa and BAEE, respectively. Trypsin-II presented an isoelectric point of 8.7, and Km values of 1.7 x 10(-4) M (BApNa) and 3.8 x 10(-5) M (BAEE). Both enzymes were differentially inhibited by some proteinase inhibitors. In particular, trypsin-I was inhibited by E-64 (ID50 = 6 microM) but not by lima bean trypsin inhibitor (LBI), whereas trypsin-II was inhibited by LBI (ID50 = 1 microM) and poorly by E-64 (ID50 = 85 microM). Changes in the susceptibility of the trypsin-like activity of midgut extracts from different larval instars to these inhibitors suggest that the relative proportion of these two enzymes varied through larval development, being predominant in early instars trypsin-I and in late instars trypsin-II.
journal_name
Insect Biochem Mol Bioljournal_title
Insect biochemistry and molecular biologyauthors
Novillo C,Castañera P,Ortego Fdoi
10.1016/s0965-1748(98)00121-0subject
Has Abstractpub_date
1999-02-01 00:00:00pages
177-84issue
2eissn
0965-1748issn
1879-0240pii
S0965174898001210journal_volume
29pub_type
杂志文章abstract::Insects taste nonvolatile chemicals through gustatory receptors (Grs) and make choices for feeding, mating, and oviposition. To date, genome projects have identified 69 Gr genes in the silkworm, Bombyx mori; however, the expression sites of these Grs remain to be explored. In this study, we used reverse transcription ...
journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
pub_type: 杂志文章
doi:10.1016/s0965-1748(97)00116-1
更新日期:1998-03-01 00:00:00
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
pub_type: 杂志文章
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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更新日期:2016-12-01 00:00:00
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journal_title:Insect biochemistry and molecular biology
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更新日期:2018-10-01 00:00:00
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journal_title:Insect biochemistry and molecular biology
pub_type: 杂志文章
doi:10.1016/j.ibmb.2010.11.002
更新日期:2011-02-01 00:00:00
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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pub_type: 杂志文章
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更新日期:1998-12-01 00:00:00
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journal_title:Insect biochemistry and molecular biology
pub_type: 杂志文章
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journal_title:Insect biochemistry and molecular biology
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更新日期:2010-10-01 00:00:00
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
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journal_title:Insect biochemistry and molecular biology
pub_type: 杂志文章
doi:10.1016/j.ibmb.2010.08.003
更新日期:2010-12-01 00:00:00
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journal_title:Insect biochemistry and molecular biology
pub_type: 杂志文章
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更新日期:2005-09-01 00:00:00
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journal_title:Insect biochemistry and molecular biology
pub_type: 杂志文章
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更新日期:2002-12-01 00:00:00
abstract::Phenoloxidases (POs) play key roles in various physiological functions in insects, e.g., cuticular sclerotization, wound healing, egg tanning, cuticle formation and melanotic encapsulaction of pathogens. Previously, we identified five POs, designated As-pro-PO I-V, from the mosquito Armigeres subalbatus and demonstrat...
journal_title:Insect biochemistry and molecular biology
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更新日期:2015-09-01 00:00:00