L-Amino acid oxidase from Naja naja oxiana venom

被引：53

作者：

Samel, Mari ^{[1
]}

Tonismagi, Kulli ^{[1
]}

Ronnholm, Gunilla ^{[2
,3
]}

Vija, Heiki ^{[1
]}

Siigur, Jueri ^{[1
]}

Kalkkinen, Nisse ^{[2
,3
]}

Siigur, Ene ^{[1
]}

机构：

[1] NICPB, EE-12618 Tallinn, Estonia

[2] Univ Helsinki, Inst Biotechnol, Prot Chem Res Grp, FIN-00014 Helsinki, Finland

[3] Univ Helsinki, Inst Biotechnol, Core Facil, FIN-00014 Helsinki, Finland

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2008年 / 149卷 / 04期

关键词：

snake venom; Naja naja oxiana; L-amino acid oxidase; platelet aggregation; antibacterial activity; partial sequencing;

D O I：

10.1016/j.cbpb.2007.11.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 degrees C, -70 degrees C) and loses its activity by heating at 70 degrees 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 mu M and 0.036 mu M, respectively. The antibacterial and anti-aggregating activity was abolished by catalase. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：572 / 580

页数：9

共 47 条

[31] BOTH NEUROTOXIN-II FROM VENOM OF NAJA-NAJA OXIANA AND ITS ENDOGENEOUS ANALOG INDUCE APOPTOSIS IN TUMOR-CELLS [J].