King T P, Kochoumian L, Joslyn A
Arch Biochem Biophys. 1984 Apr;230(1):1-12. doi: 10.1016/0003-9861(84)90080-8.
Three major venom proteins from different species of wasps have been isolated and characterized. They are hyaluronidase, phospholipase, and antigen 5 of as yet unknown biochemical function. These three proteins are allergens in wasp venom-sensitive persons. The species of wasps studied, of the genus Polistes, were annularis, carolina, exclamans, fuscatus, and instabilis. Antigen 5 and phospholipase from wasp venoms were shown to be antigenically distinct from homologous proteins of yellowjacket venoms. The venom phospholipase from wasp, as well as that from yellowjacket (Vespula germanica), appears to have dual enzymatic specificities of the A1 and B types. That is, hydrolysis takes place at the 1-acyl residue of phosphatidylcholine and at the 1- or 2-acyl residue of lysophosphatidylcholine.
已从不同种类的黄蜂中分离并鉴定出三种主要的毒液蛋白。它们是透明质酸酶、磷脂酶和生化功能尚不清楚的抗原5。这三种蛋白质是对黄蜂毒液敏感者的过敏原。所研究的黄蜂种类属于长脚黄蜂属,包括环纹长脚黄蜂、卡罗来纳长脚黄蜂、惊叫长脚黄蜂、黑褐长脚黄蜂和不稳定长脚黄蜂。黄蜂毒液中的抗原5和磷脂酶在抗原性上与黄胡蜂毒液中的同源蛋白不同。黄蜂毒液中的磷脂酶以及黄胡蜂(德国黄胡蜂)毒液中的磷脂酶似乎具有A1和B型双重酶特异性。也就是说,水解发生在磷脂酰胆碱的1-酰基残基以及溶血磷脂酰胆碱的1-或2-酰基残基处。