Huang M Z, Gopalakrishnakone P, Chung M C, Kini R M
Department of Anatomy, Department of Biochemistry, Bioscience Centre, Bioprocessing Technology Centre, National University of Singapore, Lower Kent Ridge Road, 119260, Singapore.
Arch Biochem Biophys. 1997 Feb 15;338(2):150-6. doi: 10.1006/abbi.1996.9814.
A phospholipase A2 (OHV A-PLA2) from the venom of Ophiophagus hannah (King cobra) is an acidic protein exhibiting cardiotoxicity, myotoxicity, and antiplatelet activity. The complete amino acid sequence of OHV A-PLA2 has been determined using a combination of Edman degradation and mass spectrometric techniques. OHV A-PLA2 is composed of a single chain of 124 amino acid residues with 14 cysteines and a calculated molecular weight of 13719 Da. It contains the loop of residues (62-66) found in pancreatic PLA2s and hence belongs to class IB enzymes. This pancreatic loop is between two proline residues (Pro 59 and Pro 68) and contains several hydrophilic amino acids (Ser and Asp). This region has high degree of conformational flexibility and is on the surface of the molecule, and hence it may be a potential protein-protein interaction site. A relatively low sequence homology is found between OHV A-PLA2 and other known cardiotoxic PLA2s, and hence a contiguous segment could not be identified as a site responsible for the cardiotoxic activity.
眼镜王蛇毒液中的一种磷脂酶A2(OHV A-PLA2)是一种酸性蛋白质,具有心脏毒性、肌毒性和抗血小板活性。OHV A-PLA2的完整氨基酸序列已通过埃德曼降解法和质谱技术相结合的方法确定。OHV A-PLA2由一条包含124个氨基酸残基的单链组成,有14个半胱氨酸,计算分子量为13719道尔顿。它含有在胰腺磷脂酶A2中发现的残基环(62-66),因此属于IB类酶。这个胰腺环位于两个脯氨酸残基(Pro 59和Pro 68)之间,包含几个亲水性氨基酸(丝氨酸和天冬氨酸)。该区域具有高度的构象灵活性,位于分子表面,因此可能是一个潜在的蛋白质-蛋白质相互作用位点。在OHV A-PLA2与其他已知的心脏毒性磷脂酶A2之间发现相对较低的序列同源性,因此无法确定一个连续片段作为负责心脏毒性活性的位点。