Li A W, Verpoorte J A, Lewis R G, Mahony D E
Can J Microbiol. 1982 Jul;28(7):860-73. doi: 10.1139/m82-128.
Bacteriocin 28, produced by Clostridium perfringens, was characterized by gel filtration and sodium dodecyl sulfate - polyacrylamide gel electrophoresis as a glycoprotein with a molecule weight of approximately 100,000. Density gradient centrifugation suggested a lower weight of 84,000. The bacteriocin bound firmly to phenyl-Sepharose CL-4B gel, indicating hydrophobic properties, and elution from this gel with ethylene glycol clearly separated bacteriocin from the alpha and theta toxins of C. perfringens, the latter of which was also hydrophobic. Bacteriocin 28 was immunogenic, inducing neutralizing and precipitating antibodies, and possessed three isoelectric points: 7.37, 7.05, and 5.4. Amino acid and carbohydrate analysis of the active material showed a composition of 15 amino acids and several carbohydrates. The molecule demonstrated instability with increasing purification, and several approaches to purification are described.
由产气荚膜梭菌产生的细菌素28，通过凝胶过滤和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳鉴定为一种糖蛋白，分子量约为100,000。密度梯度离心表明其分子量较低，为84,000。该细菌素与苯基-琼脂糖CL-4B凝胶紧密结合，表明具有疏水性，用乙二醇从该凝胶上洗脱可将细菌素与产气荚膜梭菌的α毒素和θ毒素清晰分离，后者也具有疏水性。细菌素28具有免疫原性，可诱导中和抗体和沉淀抗体，并有三个等电点：7.37、7.05和5.4。对活性物质的氨基酸和碳水化合物分析表明其由15种氨基酸和几种碳水化合物组成。随着纯化程度的提高，该分子表现出不稳定性，并描述了几种纯化方法。
