Igarashi H, Morita T, Iwanaga S
J Biochem. 1979 Nov;86(5):1615-8. doi: 10.1093/oxfordjournals.jbchem.a132679.
Staphylocoagulase was isolated from a culture filtrate of Staphylococcus aureus, strain st-213, by a two step purification procedure of chromatography on a bovine prothrombin-Sepharose 4B affinity column and gel filtration on Sephadex G-25. The yield of the coagulase activity ranged from 75--83% and the purified preparation gave a single precipitin line in immunodiffusion tests against anti-crude and anti-purified staphylocoagulase sera. However, the final product was shown to contain one major and two minor components by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Chemical analysis of the material indicated that it does not contain any cystine residues and that its NH2-terminal residue is a single isoleucine.
通过两步纯化程序从金黄色葡萄球菌st-213菌株的培养滤液中分离出葡萄球菌凝固酶，该程序包括在牛凝血酶原-琼脂糖凝胶4B亲和柱上进行色谱分离以及在葡聚糖凝胶G-25上进行凝胶过滤。凝固酶活性的产率在75%至83%之间，纯化后的制剂在针对抗粗制和抗纯化葡萄球菌凝固酶血清的免疫扩散试验中呈现单一沉淀线。然而，通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳显示，最终产物含有一个主要成分和两个次要成分。对该物质的化学分析表明，它不含有任何胱氨酸残基，并且其氨基末端残基是单个异亮氨酸。
