Barberio C, Delfino G, Mastromei G
Dipartimento di Biologia animale e Genetica, Università degli Studi di Firenze, Italy.
Toxicon. 1987;25(8):899-909. doi: 10.1016/0041-0101(87)90250-9.
The cutaneous 'venom' was collected from dorsal skin fragments of the yellow-bellied toad Bombina variegata pachypus by means of stimulation with noradrenaline. Light and electron microscope observations gave evidence that the 'venom' corresponds to the secretory products of both serous gland types (i.e. with small or large granules) characteristic of this genus, which had discharged their contents upon stimulation. The serous 'venom', when tested for antimicrobial activity, inhibited the growth of several bacterial strains. Heat treatment, dialysis, protease digestion and SDS-PAGE electrophoresis showed that the antimicrobial activity was thermostable and associated with a low molecular weight protein. This protein was purified and homogeneity determined by CM-cellulose chromatography and SDS-PAGE electrophoresis. The purified protein has a molecular weight of 6700, displays antibacterial properties and appears different from the antimicrobially active peptides previously isolated from the 'venom' of the toad.
通过用去甲肾上腺素刺激，从黄腹蟾蜍（Bombina variegata pachypus）的背部皮肤碎片中收集皮肤“毒液”。光学显微镜和电子显微镜观察表明，这种“毒液”对应于该属特有的两种浆液腺类型（即含小颗粒或大颗粒的）的分泌产物，这些腺体在受到刺激时已排出其内容物。当检测浆液性“毒液”的抗菌活性时，它抑制了几种细菌菌株的生长。热处理、透析、蛋白酶消化和SDS-PAGE电泳表明，抗菌活性是热稳定的，并且与一种低分子量蛋白质有关。该蛋白质经过纯化，并通过CM-纤维素色谱法和SDS-PAGE电泳确定其均一性。纯化后的蛋白质分子量为6700，具有抗菌特性，并且似乎与先前从蟾蜍“毒液”中分离出的具有抗菌活性的肽不同。
