Phosphatidylinositol-specific phospholipase C From Bacillus cereus: Improved purification, amino acid composition, and amino-terminal sequence

✍ Scribed by Johannes J. Volwerk; Peter B. Wetherwax; Loreene M. Evans; Andreas Kuppe; O. Hayes Griffith

• Book ID: 102876225
• Publisher: John Wiley and Sons
• Year: 1989
• Tongue: English
• Weight: 672 KB
• Volume: 39
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.240390311

✦ Synopsis

Phosphatidylinositol-specific phospholipase C was purified in a 27 % yield from the culture medium of Bacillus cereus by a combination of ammonium sulfate precipitation and ion-exchange and hydrophobic interaction chromatography. The purified enzyme was free of other phospholipase C-type activities and exhibited a high specific activity of approximately 1,300 unitdmg. Amino acid composition analysis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated a molecular weight of about 35 kDa. The sequence of the first 29 N-terminal amino acids was also determined.