Title: Characterization of four substrates emphasizes kinetic similarity between insect and human C-domain angiotensin-converting enzyme
Authors: Hens, Korneel
Vandingenen, Anick
Macours, Nathalie
Baggerman, Geert
Karaoglanovic, A.C.
Schoofs, Liliane
De Loof, Arnold
Huybrechts, Roger # ×
Issue Date: 2002
Publisher: Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Series Title: European Journal of Biochemistry vol:269 issue:14 pages:3522-3530
Abstract: Angiotensin converting enzyme (ACE) was already discovered in insects in 1994, but its physiological role is still enigmatic. We have addressed this problem by purifying four new ACE substrates from the ovaries of the grey fleshfly, Neobellieria bullata . Their primary structures were identified as NKLKPSQWISLSD (Neb -ODAIF- 1(1-13) ), NKLKPSQWI (Neb -ODAIF- 1(1-9) ), SLKPSNWLTPSE (Neb -ODAIF- 2) and LEQIYHL. Database analysis showed significant homology with amino acid sequence stretches as present in the N-terminal part of several fly yolk proteins. An antiserum raised against Neb -ODAIF-1(1-9) immunostained one out of three yolk protein bands of SDS/PAGE-separated fly haemolymph and egg homogenate, thus confirming that these peptides originate from a yolk protein gene product. Kinetic analysis of these peptides and of the peptides Neb -ODAIF and Neb -ODAIF- 1(1-7) with insect ACE and human ACE show both similar and unique properties for insect ACE as compared with human C-domain ACE.
ISSN: 0014-2956
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Department of Biology - miscellaneous
Microbial and Molecular Systems - miscellaneous
Animal Physiology and Neurobiology Section - miscellaneous
× corresponding author
# (joint) last author

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