A family of peptides with broad-spectrum antimicrobial activity has been isolated from the skin of the African clawed frog Xenopus laevis. It consists of two closely related peptides that are each 23 amino acids and differ by two substitutions. These peptides are water soluble, nonhemolytic at their effective antimicrobial concentrations, and potentially amphiphilic. At low concentrations they inhibit growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. The sequence of a partial cDNA of the precursor reveals that both peptides derive from a common larger protein. These peptides appear to represent a previously unrecognized class of vertebrate antimicrobial activities.

中文翻译：

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Magainins是非洲爪蟾皮肤的一类抗菌肽：分离，两种活性形式的表征以及前体的部分cDNA序列。

从非洲爪蛙非洲爪蟾的皮肤中分离出了具有广谱抗菌活性的肽家族。它由两个紧密相关的肽组成，每个肽均为23个氨基酸，相差两个取代。这些肽是水溶性的，在其有效的抗菌浓度下不溶血，并且可能是两亲的。在低浓度下，它们抑制多种细菌和真菌的生长，并诱导原生动物的渗透裂解。前体的部分cDNA序列显示这两个肽均来自共同的较大蛋白。这些肽似乎代表了以前无法识别的脊椎动物抗菌活性。