Abstract
A new Phospholipase A2 (PLA2) from Micrurus dumerilii carinicauda venom was isolated and its primary structure determined. This new PLA2 showed a low enzymatic activity when compared with other PLA2s and it is moderately basic with an isoelectric point of 8.0. Its amino acid sequence showed the presence of 120 amino acid residues and its sequence was: NLIQFLNMIQCTTPGREPLVAFANYGCYCGRGGSGTPVDELDRCCQVHDNCYDTAKKVFGCSPYFTMYSYDCSEGKLTCKDNNTKCKAAVCNCDRTAALCFAKAPYNDKNYKIDLTKRCQ. The structural model of MIDCA1, when compared with other strong neurotoxic PLA2s, such as Naja naja, showed significant differences in the β-wing and neurotoxic sites, despite the high level of amino acid sequence similarity. These observations indicate a dissociation between the biological and catalytic activity of this new PLA2, supporting the view that other regions of the protein are involved in the biological effects.
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Abbreviations
- MIDCA1:
-
Micrurus dumerilli carinicauda phospholipase A2 1
- HPLC:
-
High performance liquid chromatography
- TFA:
-
trifluoroacetic acid
- MALDI TOF:
-
Matrix Assisted Laser Desorption/Ionization Time-Of-Fligh
- EDTA:
-
Ethylenediaminetetraacetic acid
- CNBr:
-
cianogen bromide
- CRD:
-
Complementarity-determining region
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Belo, C.A.D., Toyama, M.H., Toyama, D.d.O. et al. Determination of the Amino Acid Sequence of a New Phospholipase A2 (MIDCA1) Isolated from Micrurus dumerilii carinicauda Venom. Protein J 24, 147–153 (2005). https://doi.org/10.1007/s10930-005-7838-1
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DOI: https://doi.org/10.1007/s10930-005-7838-1