The metal ion dependence of phospholipase C from Bacillus cereus.

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

1. The zinc content and metal ion dependence of phospholipase C(phosphatidylcholine cholinephosphohydrolase, EC 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.

Product Number
Product Description

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

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.