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

European Journal of Entomology

Constant GIELENS¹  Liliane SCHOOFS²  Korneel HENS²  Geert BAGGERMAN²  Roger HUYBRECHTS²  Nathalie MACOURS²  Anick VANDINGENEN² 

[1] Laboratory of Biochemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200G, B-3001 Leuven-Heverlee, Belgium;Laboratory of Developmental Physiology and Molecular Biology, Katholieke Universiteit Leuven, Naamsestraat 59, B-3000 Leuven, Belgium;

关键词: ace inhibitors;    cdna cloning;    insects;    locusta migratoria;    reproduction;    testes;   

DOI  :  10.14411/eje.2003.070

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown