Complete purification of phosphatidylinositol-specific phospholipase C from a strain of Bacillus thuringiensis.
A phosphatidylinositol-specific phospholipase C was purified from the culture broth of Bacillus thuringiensis IAM 12077 to a homogeneous state as revealed by polyacrylamide gel electrophoresis. The specific activity of the purified enzyme was 559 units/mg and recovery of the enzyme activity was 31%. Molecular and physiological properties of the purified enzyme, including molecular weight (22,000), isoelectric point (pI = 4.9) and its ectoenzyme-releasing activity, were studied in comparison with those other known enzymes of bacterial origin.
D001413:Bacillus thuringiensis / Q000201:enzymology*; D007526:Isoelectric Point; D008970:Molecular Weight; D010716:Phosphatidylinositols; D010740:Phospholipases / Q000302:isolation & purification*; D010738:Type C Phospholipases / Q000302:isolation & purification*
D010716:Phosphatidylinositols; D010740:Phospholipases; D010738:Type C Phospholipases