title: Phosphatidylinositol-specific phospholipase C from Bacillus cereus: improved purification, amino acid composition, and amino-terminal sequence.
abstract: 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 units/mg. 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.
authors.affiliation: Institute of Molecular Biology, University of Oregon, Eugene 97403.
authors.forename: J J
authors.initials: JJ
authors.lastname: Volwerk
authors.forename: P B
authors.initials: PB
authors.lastname: Wetherwax
authors.forename: L M
authors.initials: LM
authors.lastname: Evans
authors.forename: A
authors.initials: A
authors.lastname: Kuppe
authors.forename: O H
authors.initials: OH
authors.lastname: Griffith
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis*; D001409:Bacillus cereus / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010716:Phosphatidylinositols / Q000378:metabolism*; D010738:Type C Phospholipases / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D010716:Phosphatidylinositols; D010738:Type C Phospholipases