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Degradation of Manduca sexta allatostatin and allatotropin by proteases associated with the foregut of Lacanobia oleracea larvae.

Abstract：

:The degradation of synthetic Manduca sexta allatostatin (Manse-AS) and allatotropin (Manse-AT), by enzymes of the foregut of larvae of the tomato moth, Lacanobia oleracea was investigated using reversed-phase high performance liquid chromatography (RP-HPLC) together with matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) and Edman sequencing. Metabolism of 1nmol Manse-AS by foregut extract (1microg protein) was rapid, t(1/2) approximately 5min, with two major products produced. Mass spectrometry of HPLC fractions identified cleavage products Manse-AS-(4-15) and Manse-AS-(6-15), which indicates enzymatic cleavage at the C-terminal side of arginine residues (R(3) and R(5)). This degradation of Manse-AS could be inhibited by up to 80% by the serine protease inhibitor aprotinin, but not PMSF, pepstatin, E64, EDTA, or 1,10-phenanthroline.M. sexta allatotropin was also rapidly degraded when incubated with foregut extract, t(1/2) approximately 8min, producing two metabolic products, one of which was identified as Manse-AT-(1-11), showing enzymatic cleavage at the C-terminal side of arginine (R(11)). The second product was identified as Manse-AT-(1-8). Hydrolysis of Manse-AT could only be partially inhibited by high doses of aprotinin (30%).

journal_name

Peptides

journal_title

Peptides

authors

Audsley N,Weaver RJ,Edwards JP

doi

10.1016/s0196-9781(02)00189-4

subject

Has Abstract

pub_date

2002-11-01 00:00:00

pages

2015-23

issue

11

eissn

0196-9781

issn

1873-5169

pii

S0196978102001894

journal_volume

23

pub_type

杂志文章

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