Literature DB >> 171093

The activation of phospholipase C from Clostridium Welchii by quinine: an absolute requirement for calcium ions.

R Klein, N Miller, P Kemp, H Laser.   

Abstract

Quinine activates the hydrolysis of phosphatidyl choline suspensions by phospholipase C (E.C. 3.1.4.3) obtained from Clostridium welchii. Low levels of calcium are an absolute requirement for this activation: Mg2+, Ba2+, Sr2+, and Zn2+ are ineffective. The induction period, or lag phase for this enzyme is dependent upon both calcium concentration and substrate interfacial surface area. At low concentrations (less then 50 muM) calcium ions affect the induction period but not the maximal rate of hydrolysis, whereas guinine predominantly affects the rate of hydrolysis by alterations in the surface charge carried by the substrate.

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Year:  1975        PMID： 171093     DOI： 10.1016/0009-3084(75)90027-4

Source DB:  PubMed          Journal:  Chem Phys Lipids        ISSN： 0009-3084            Impact factor:   3.329


  4 in total

1.  Validation of a simple radiochemical assay measuring hydrolysis of choline-labelled microsomal phosphatidylcholine by phospholipase C. pH-dependence.

Authors:  B R Cater; P Trivedi; T Hallinan
Journal:  Biochem J       Date:  1976-12-15       Impact factor: 3.857

2.  On the question of an electrokinetic requirement for phospholipase C action.

Authors:  R M Dawson; N L Hemington; N G Miller; A D Bangham
Journal:  J Membr Biol       Date:  1976-10-20       Impact factor: 1.843

3.  Phosphatidylethanolamine synthesis by castor bean endosperm : membrane bilayer distribution of phosphatidylethanolamine synthesized by the ethanolaminephosphotransferase and ethanolamine exchange reactions.

Authors:  S Shin; T S Moore
Journal:  Plant Physiol       Date:  1990-05       Impact factor: 8.340

Review 4.  Bacterial phospholipases C.

Authors:  R W Titball
Journal:  Microbiol Rev       Date:  1993-06
  4 in total

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