Park C B, Kim M S, Kim S C
Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejeon, Korea.
Biochem Biophys Res Commun. 1996 Jan 5;218(1):408-13. doi: 10.1006/bbrc.1996.0071.
A potent and structurally novel antimicrobial peptide was isolated and characterized from the stomach tissue of Bufo bufo gargarizans, an Asian toad. The 39-amino acid peptide, named buforin I, was purified to homogeneity by heparin-affinity column and reverse-phase HPLC. The amino acid sequence of buforin I was identical in 37 of 39 amino-terminal residues of Xenopus histone H2A. The buforin I showed strong antimicrobial activities in vitro against a broad-spectrum of microorganisms and was found to be more potent than magainin 2. In addition, a 21-amino acid peptide, named buforin II, which was derived from buforin I, showed more potent antimicrobial activities than buforin I.
从亚洲蟾蜍中华大蟾蜍的胃组织中分离并鉴定出一种强效且结构新颖的抗菌肽。这种由39个氨基酸组成的肽名为蟾蜍 Buforin I，通过肝素亲和柱和反相高效液相色谱法纯化至同质。Buforin I 的氨基酸序列在非洲爪蟾组蛋白H2A 的39个氨基末端残基中的37个上是相同的。Buforin I 在体外对多种微生物表现出强大的抗菌活性，并且发现其比蛙皮抗菌肽2更有效。此外，一种源自Buforin I 的由21个氨基酸组成的肽Buforin II，表现出比Buforin I 更强的抗菌活性。
