Kamata K, Arai Y, Kasuya Y, Aoki Y, Samejima Y
Department of Pharmacology, School of Pharmacy, Hoshi University, Tokyo, Japan.
Res Commun Chem Pathol Pharmacol. 1991 Dec;74(3):375-8.
The pharmacological activities of Trimeresurus flavoviridis phospholipase A2 (PLA2) and their chemically-modified PLA2 were characterized by measuring the contraction of rat stomach fundus strips. The native PLA2 produced a contraction of rat fundus strips. The alpha-amino-modified enzyme induced an almost identical contraction of the fundus with that of the native enzyme, whereas His-modified and Lys-modified enzymes induced a markedly decreased contraction as compared with the native enzyme. These results demonstrate that lysine and histidine residues but not the alpha-amino group in the PLA2 molecule are essential for contractile activity of the stomach fundus.
通过测量大鼠胃底条的收缩来表征竹叶青磷脂酶A2（PLA2）及其化学修饰的PLA2的药理活性。天然PLA2可使大鼠胃底条收缩。α-氨基修饰的酶诱导的胃底收缩与天然酶几乎相同，而组氨酸修饰和赖氨酸修饰的酶与天然酶相比，诱导的收缩明显降低。这些结果表明，PLA2分子中的赖氨酸和组氨酸残基而非α-氨基对于胃底的收缩活性至关重要。
