L-Amino acid oxidase from Naja naja oxiana venom |
| |
Authors: | Samel Mari Tõnismägi Külli Rönnholm Gunilla Vija Heiki Siigur Jüri Kalkkinen Nisse Siigur Ene |
| |
Institution: | aNational Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia;bProtein Chemistry Research Group and Core Facility, Institute of Biotechnology, FIN-00014 University of Helsinki, Finland |
| |
Abstract: | A new l-amino acid oxidase (LAAO) was isolated from the Central Asian cobra Naja naja oxiana venom by size exclusion, ion exchange and hydrophobic chromatography. The N-terminal sequence and the internal peptide sequences share high similarity with other snake venom l-amino acid oxidases, especially with those isolated from elapid venoms. The enzyme is stable at low temperatures (− 20 °C, − 70 °C) and loses its activity by heating at 70 °C. Specific substrates for the isolated protein are l-phenylalanine, l-tryptophan, l-methionine and l-leucine. The enzyme has antibacterial activity inhibiting the growth of Gram-positive (Bacillus subtilis) and Gram-negative (Escherichia coli) bacteria. N. naja oxiana LAAO dose-dependently inhibited ADP- or collagen-induced platelet aggregation with IC50 of 0.094 μM and 0.036 μM, respectively. The antibacterial and anti-aggregating activity was abolished by catalase. |
| |
Keywords: | Snake venom Naja naja oxiana l-Amino acid oxidase" target="_blank">l-Amino acid oxidase Platelet aggregation Antibacterial activity Partial sequencing |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|