Shol'ts K F, Reznik G I, Solov'eva N A, Shezhkova L G, Miroshnikov A I
Biokhimiia. 1980 Oct;45(10):1840-9.
The uncoupling effect of melittin, the principal peptide of bee venom was studied. It was found that the activation of mitochondrial respiration by melittin and its derivative is due to the formation of channels equally penetrable for lithium, sodium, potassium and rubidium ions. The penetrability of the inner mitochondrial membrane appears at melittin or tetraacetyl melittin concentrations about 0.90 or 0.15 nmol/mg of protein, respectively. The appreciable increase of the uncoupling activity of melittin under blocking of its amino groups suggests that these groups are not very essential for the channel formation. In contrast to gramicidin S and similar to gramicidin A, the effect of melittin develops in time. The lag in the effects of melittin and its derivative indicates that the slow rearrangement stage precedes the formation of channels in the membrane. It is suggested that the effects of melittin are due to the formation of multimolecular complexes of the peptide with phosphatides of the inner mitochondrial membrane.
对蜂毒主要肽成分蜂毒肽的解偶联作用进行了研究。研究发现，蜂毒肽及其衍生物对线粒体呼吸的激活作用是由于形成了对锂、钠、钾和铷离子具有同等通透性的通道。线粒体内膜的通透性分别在蜂毒肽或四乙酰蜂毒肽浓度约为0.90或0.15 nmol/mg蛋白质时出现。蜂毒肽氨基被阻断时其解偶联活性显著增加，这表明这些基团对通道形成并非非常关键。与短杆菌肽S不同，与短杆菌肽A相似，蜂毒肽的作用随时间发展。蜂毒肽及其衍生物作用的延迟表明，在膜中通道形成之前存在缓慢的重排阶段。有人提出，蜂毒肽的作用是由于该肽与线粒体内膜磷脂形成多分子复合物所致。
