Search for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria.
An HPLC analysis of hemolymph extracts was undertaken to uncover differences between desert locusts, Schistocerca gregaria, reared under either crowded or isolated conditions. Some differences in the chromatographic pattern could be detected. One of the major peaks in the hemolymph of crowd-reared a...
Main Authors: | , , , , , , , , , , |
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Format: | Journal article |
Language: | English |
Published: |
2002
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author | Rahman, M Bosch, L Baggerman, G Clynen, E Hens, K Hoste, B Meylaers, K Vercammen, T Schoofs, L De Loof, A Breuer, M |
author_facet | Rahman, M Bosch, L Baggerman, G Clynen, E Hens, K Hoste, B Meylaers, K Vercammen, T Schoofs, L De Loof, A Breuer, M |
author_sort | Rahman, M |
collection | OXFORD |
description | An HPLC analysis of hemolymph extracts was undertaken to uncover differences between desert locusts, Schistocerca gregaria, reared under either crowded or isolated conditions. Some differences in the chromatographic pattern could be detected. One of the major peaks in the hemolymph of crowd-reared adults was found to be a minor one in isolated-reared individuals, whereas other peaks increased after solitarization. The differences became even more pronounced after several generations of isolated rearing. The dominant chromatographic peak in hemolymph extracts of the crowd-reared animals was identified as a novel peptide with a molecular mass of 6080Da. Edman degradation in combination with enzymatic fragmentation and quadrupole-time of flight (Q-Tof) mass spectrometry revealed the full sequence: DNADEDTICVAADNKFYLYANSLKLYTCYNQLPKVYVVKPKSQCRSSLSDCPTS. This 54 aa-peptide is very abundant in hemolymph of crowd-reared adults. Its concentration in hemolymph amounts to 0.1mM. To uncover the function, its effects were investigated in several bioassays, so far without positive results. One of the other peaks differentially expressed in the individuals of the two phases was identified as SGPI-2 (MW=3794Da), which is a serine protease inhibitor in locusts. |
first_indexed | 2024-03-07T00:20:32Z |
format | Journal article |
id | oxford-uuid:7c656cfa-1acb-4935-9acc-592b318f897b |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T00:20:32Z |
publishDate | 2002 |
record_format | dspace |
spelling | oxford-uuid:7c656cfa-1acb-4935-9acc-592b318f897b2022-03-26T20:56:49ZSearch for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:7c656cfa-1acb-4935-9acc-592b318f897bEnglishSymplectic Elements at Oxford2002Rahman, MBosch, LBaggerman, GClynen, EHens, KHoste, BMeylaers, KVercammen, TSchoofs, LDe Loof, ABreuer, MAn HPLC analysis of hemolymph extracts was undertaken to uncover differences between desert locusts, Schistocerca gregaria, reared under either crowded or isolated conditions. Some differences in the chromatographic pattern could be detected. One of the major peaks in the hemolymph of crowd-reared adults was found to be a minor one in isolated-reared individuals, whereas other peaks increased after solitarization. The differences became even more pronounced after several generations of isolated rearing. The dominant chromatographic peak in hemolymph extracts of the crowd-reared animals was identified as a novel peptide with a molecular mass of 6080Da. Edman degradation in combination with enzymatic fragmentation and quadrupole-time of flight (Q-Tof) mass spectrometry revealed the full sequence: DNADEDTICVAADNKFYLYANSLKLYTCYNQLPKVYVVKPKSQCRSSLSDCPTS. This 54 aa-peptide is very abundant in hemolymph of crowd-reared adults. Its concentration in hemolymph amounts to 0.1mM. To uncover the function, its effects were investigated in several bioassays, so far without positive results. One of the other peaks differentially expressed in the individuals of the two phases was identified as SGPI-2 (MW=3794Da), which is a serine protease inhibitor in locusts. |
spellingShingle | Rahman, M Bosch, L Baggerman, G Clynen, E Hens, K Hoste, B Meylaers, K Vercammen, T Schoofs, L De Loof, A Breuer, M Search for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria. |
title | Search for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria. |
title_full | Search for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria. |
title_fullStr | Search for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria. |
title_full_unstemmed | Search for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria. |
title_short | Search for peptidic molecular markers in hemolymph of crowd-(gregarious) and isolated-reared (solitary) desert locusts, Schistocerca gregaria. |
title_sort | search for peptidic molecular markers in hemolymph of crowd gregarious and isolated reared solitary desert locusts schistocerca gregaria |
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