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Activity and mechanism of action of insect oostatic peptides in flesh fly.

Authors
  • Slaninová, Jirina
  • Bennettová, Blanka
  • Nazarov, Elsan S
  • Simek, Petr
  • Holík, Josef
  • Vlasáková, Vera
  • Hlavácek, Jan
  • Cerný, Bohuslav
  • Tykva, Richard
Type
Published Article
Journal
Bioorganic chemistry
Publication Date
Aug 01, 2004
Volume
32
Issue
4
Pages
263–273
Identifiers
PMID: 15210340
Source
Medline
License
Unknown

Abstract

The relationship between structure and activity of insect oostatic decapeptide (Aed-TMOF) analogues in flesh fly was analyzed. The highest oostatic activity was exhibited by the pentapetide and tetrapeptide analogues, H-Tyr-Asp-Pro-Ala-Pro-OH and H-Tyr-Asp-Pro-Ala-OH, respectively. The tetrapeptide, either native or tritiated, was used to study its metabolism in the ovaries and hemolymph and to detect putative binding sites in the flesh fly ovaries and head. A high metabolism of the tetrapeptide with a half-life in the hemolymph and ovaries less than 1h was determined. The initial limiting step in the degradation is tyrosine(1) cleavage. Other degradation products were detected only transiently in low quantities. Using tritiated tetrapeptide, we found that only very low specific binding was detected in the homogenates of ovaries and in the rough membrane preparation in the presence and absence of protease inhibitors.

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