PURIFICATION AND CHARACTERIZATION OF THERMOSTABLE DIRECT HEMOLYSIN OF VIBRIO-PARAHAEMOLYTICUS
PURIFICATION AND CHARACTERIZATION OF THERMOSTABLE DIRECT HEMOLYSIN OF VIBRIO-PARAHAEMOLYTICUS
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DOI：
10.1128/iai.8.5.775-780.1973
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发表时间：
1973-01-01
影响因子：
3.1
通讯作者：
MIWATANI, T
中科院分区：
文献类型：
--
作者：
SAKURAI, J;MATSUZAKI, A;MIWATANI, T
从副溶血性弧菌（Vibrio parahaemolyticus）培养物中分离纯化出一种耐热的直接溶血素，该溶血素与抗溶血素抗血清在琼脂扩散试验中有一条沉淀线，在聚丙烯酰胺凝胶电泳中有一条带。溶血素在70 ~ 100 ℃加热10分钟不能失活。加入卵磷脂不能提高溶血活性。证明溶血素是分子量约为118，000的蛋白质。氨基酸分析表明，总氨基酸的43%是酸性氨基酸，而11%是碱性氨基酸。
A thermostable direct hemolysin was purified from culture filtrates ofVibrio parahaemolyticus.The purified hemolysin gave one precipitation line with the antihemolysin antiserum on agar-gel diffusion test and a single band on polyacrylamide gel electrophoresis. The hemolysin was not inactivated by heating at 70 to 100 C for 10 min. The hemolytic activity was not enhanced by the addition of lecithin. It was demonstrated that the hemolysin was a protein with a molecular weight of approximately 118,000. Amino acid analysis revealed that 43% of total amino acids were acidic amino acids, whereas 11% were basic amino acids.