绵羊棒状杆菌外毒素的纯化及部分特性鉴定
Purification and partial characterization of the exotoxin of Corynebacterium ovis.
作者信息
Onon E O
出版信息
Biochem J. 1979 Jan 1;177(1):181-6. doi: 10.1042/bj1770181.
Abstract
- The toxin from Corynebacterium ovis, a phospholipase D (sphingomyelin phosphodiesterase D) that acts on 2-lysophosphatidylcholine and sphingomyelins, was purified by about 400-fold to homogeneity as judged by several criteria. [The EC number of the toxin (EC 3.1.4.41) has been allotted by the Nomenclature Committee of IUB, but has not yet been published.] 2. A new assay method performed in vitro, based on inhibition by the toxin of erythrocyte lysis by staphylococcal beta-haemolysin, was developed to facilitate the purification. 3. The toxin was found to be a basic (pI9.1) glycoprotein of mol.wt. 14,500 +/- 1,000. 4. The amino acid composition of the toxin was highly reminiscent of that of collagen, since it contained hydroxyproline, hydroxylysine and a high proportion of glycine, but preliminary tests showed no other similarities to collagen or proteins with similar compositions.
摘要
- 绵羊棒状杆菌产生的毒素是一种磷脂酶D（鞘磷脂磷酸二酯酶D），作用于2-溶血磷脂酰胆碱和鞘磷脂，通过多种标准判断，该毒素已纯化至约400倍的纯度，达到均质状态。[该毒素的酶委员会编号（EC 3.1.4.41）已由国际生物化学与分子生物学联盟命名委员会指定，但尚未公布。] 2. 开发了一种基于毒素抑制葡萄球菌β-溶血素引起的红细胞溶解的体外新检测方法，以促进纯化过程。3. 发现该毒素是一种碱性（pI9.1）糖蛋白，分子量为14,500±1,000。4. 该毒素的氨基酸组成与胶原蛋白的氨基酸组成高度相似，因为它含有羟脯氨酸、羟赖氨酸和高比例的甘氨酸，但初步测试表明，它与胶原蛋白或具有相似组成的蛋白质没有其他相似之处。
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