摘要
采用固相法设计合成了４个蜂毒肽片段：Ｍｅｌ１２、Ｍｅ１１３、Ｍｅｌ１４、Ｍｅｌ１５。应用电泳技术，抑制钙依赖性的磷酸二酯酶酶活方法和荧光技术研究了这些多肽与钙调蛋白的相互作用。结果表明这些多肽与钙调蛋白均形成１：１复合物，抑制钙依赖性的磷酸二酯酶的活性，其中Ｍｅｌ１４和Ｍｅｌ１５对钙调蛋白的结合活性与完整的蜂毒肽比较接近。
Four fragments of melittin were manually synthesized by standard solid-phase method: Mel 12, Mel 13, Mel 14 and Mel 15. Their interaction with calmodulin was studied by electrophoresis method, inhibited activity of Ca￣(2+)-dependent 3', 5'-cAMP phosphodiesterase and flurescence technique.The results show that these peptides form 1: 1 complex with calmodulin and inhibit the activity of phosphodiesterase. Among these peptides, Mel 14 and Mel 15 have almost the same binding activity with calmodulin as the intact peptide Melittin.
出处
《生物化学杂志》
CAS
CSCD
1994年第6期651-656,共6页
基金
国家青年科学基金
南开大学科学技术发展基金
关键词
蜂毒肽
片段
调钙蛋白
合成
Calmodulin
Fragment of melittin
Solid-phase synthesis.
