Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)

By means of a tracer assay using a labeled synthetic angiotensin converting enzyme (ACE) substrate hippurylglycylglycine, we have detected high ACE activity in the testes of the African migratory locust, Locusta migratoria. Lower, but significant, ACE activity was observed in midgut and hemolymph. I...

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Main Authors: Macours, N, Vandingenen, A, Gielens, C, Hens, K, Baggerman, G, Schoofs, L, Huybrechts, R
Format: Journal article
Language:English
Published: 2003
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author Macours, N
Vandingenen, A
Gielens, C
Hens, K
Baggerman, G
Schoofs, L
Huybrechts, R
author_facet Macours, N
Vandingenen, A
Gielens, C
Hens, K
Baggerman, G
Schoofs, L
Huybrechts, R
author_sort Macours, N
collection OXFORD
description By means of a tracer assay using a labeled synthetic angiotensin converting enzyme (ACE) substrate hippurylglycylglycine, we have detected high ACE activity in the testes of the African migratory locust, Locusta migratoria. Lower, but significant, ACE activity was observed in midgut and hemolymph. In a two-step purification procedure involving anion exchange and gel permeation chromatography, we have purified LomACE from the locust testes. The enzyme of approximately 80 kDa shows substantial amino-acid sequence homology with ACE from both vertebrate and invertebrate origin. The ACE identity of the purified enzyme was further confirmed by cDNA cloning of the Locusta ACE fragment, which, after in silico translation, revealed a mature protein of 623 amino acids with a large structural similarity to other known ACE proteins.
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spelling oxford-uuid:45277b3d-6abb-4ff1-982c-b19185cfbea22022-03-26T15:06:07ZIsolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:45277b3d-6abb-4ff1-982c-b19185cfbea2EnglishSymplectic Elements at Oxford2003Macours, NVandingenen, AGielens, CHens, KBaggerman, GSchoofs, LHuybrechts, RBy means of a tracer assay using a labeled synthetic angiotensin converting enzyme (ACE) substrate hippurylglycylglycine, we have detected high ACE activity in the testes of the African migratory locust, Locusta migratoria. Lower, but significant, ACE activity was observed in midgut and hemolymph. In a two-step purification procedure involving anion exchange and gel permeation chromatography, we have purified LomACE from the locust testes. The enzyme of approximately 80 kDa shows substantial amino-acid sequence homology with ACE from both vertebrate and invertebrate origin. The ACE identity of the purified enzyme was further confirmed by cDNA cloning of the Locusta ACE fragment, which, after in silico translation, revealed a mature protein of 623 amino acids with a large structural similarity to other known ACE proteins.
spellingShingle Macours, N
Vandingenen, A
Gielens, C
Hens, K
Baggerman, G
Schoofs, L
Huybrechts, R
Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)
title Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)
title_full Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)
title_fullStr Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)
title_full_unstemmed Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)
title_short Isolation of angiotensin converting enzyme from testes of Locusta migratoria (Orthoptera)
title_sort isolation of angiotensin converting enzyme from testes of locusta migratoria orthoptera
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