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

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.

journal_name

Bioorg Chem

journal_title

Bioorganic chemistry

authors

Slaninová J,Bennettová B,Nazarov ES,Simek P,Holík J,Vlasáková V,Hlavácek J,Cerný B,Tykva R

doi

10.1016/j.bioorg.2004.05.003

subject

Has Abstract

pub_date

2004-08-01 00:00:00

pages

263-73

issue

4

eissn

0045-2068

issn

1090-2120

pii

S0045206804000306

journal_volume

32

pub_type

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