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来自中亚眼镜蛇毒液的L-氨基酸氧化酶。

L-Amino acid oxidase from Naja naja oxiana venom.

作者信息

Samel Mari, Tõnismägi Külli, Rönnholm Gunilla, Vija Heiki, Siigur Jüri, Kalkkinen Nisse, Siigur Ene

机构信息

National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia.

出版信息

Comp Biochem Physiol B Biochem Mol Biol. 2008 Apr;149(4):572-80. doi: 10.1016/j.cbpb.2007.11.008. Epub 2007 Nov 28.

DOI:10.1016/j.cbpb.2007.11.008
PMID:18294891
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 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 IC(50) of 0.094 microM and 0.036 microM, respectively. The antibacterial and anti-aggregating activity was abolished by catalase.

摘要

通过尺寸排阻色谱、离子交换色谱和疏水色谱从中亚眼镜蛇(Naja naja oxiana)毒液中分离出一种新型L-氨基酸氧化酶(LAAO)。该酶的N端序列和内部肽段序列与其他蛇毒L-氨基酸氧化酶高度相似,尤其是与从眼镜蛇科毒液中分离出的那些酶。该酶在低温(-20℃、-70℃)下稳定,在70℃加热会失去活性。分离出的该蛋白的特异性底物为L-苯丙氨酸、L-色氨酸、L-甲硫氨酸和L-亮氨酸。该酶具有抗菌活性,可抑制革兰氏阳性菌(枯草芽孢杆菌)和革兰氏阴性菌(大肠杆菌)的生长。中亚眼镜蛇LAAO对ADP或胶原诱导的血小板聚集具有剂量依赖性抑制作用,IC50分别为0.094 microM和0.036 microM。过氧化氢酶可消除其抗菌和抗聚集活性。

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