The metal ion dependence of phospholipase C from Bacillus cereus.

Biochimica et biophysica acta (1975-06-24)
C Little, A B Otnåss
PMID807246
ABSTRACT

1. The zinc content and metal ion dependence of phospholipase C(phosphatidylcholine cholinephosphohydrolase, EC 3.1.4.3) from Bacillus cereus have been examined. 2. The native enzyme contained about 2 atoms of tightly bound zinc/molecule. 3. Incubation of the enzyme with EDTA or with o-phenanthroline caused inactivation. The inactivation was accompanied by the removal of one zinc atom from the enzyme and could be fully reversed by the addition of Zn2+ or Co2+ to the enzyme and partly reversed by Mn2+ or Mg2+. 4. Prolonged exposure to o-phenanthroline removed the second zinc atom also and produced an enzyme species which was reactivated by Zn2+ only. Full reactivation was accompanied by the binding of about two zinc atoms to the enzyme. 5. The results are consistent with the view that phospholipase C is a zinc metalloenzyme.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Phospholipase C from Clostridium perfringens (C. welchii), Type I, lyophilized powder, 10-50 units/mg protein
Sigma-Aldrich
Phospholipase C from Bacillus cereus, ≥200 units/mg protein
Sigma-Aldrich
Phospholipase C from Clostridium perfringens (C. welchii), Type XIV, lyophilized powder, ≥150 units/mg protein

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