Modulation of erythrocyte acetylcholinesterase by cardiolipin: Effect on subunit coupling revealed by irradiation inactivation |
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Authors: | Guy Beauregard Michel Potier Basil D Roufogalis |
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Institution: | 1. Section de Génétique Médicale, Centre de Recherche Pédiatrique, Hôpital Sainte-Justine, Université de Montréal, Montréal, Québec, Canada H3T 1C5;2. Laboratory of Molecular Pharmacology, Faculty of Pharamceutical Sciences, University of British Columbia, Vancouver, B.C., Canada V6T 1W5 |
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Abstract: | The functional molecular weights of two kinetically distinct forms of bovine erythrocyte acetylcholinesterase were determined by irradiation inactivation. Whereas both forms have similar molecular weights by hydrodynamic measurements and contain 33 molecules of cardiolipin, the functional molecular weight of form α (140,000) was found to be twice that of form β (73,000). As form β is derived from form α by treatment with high salt concentration in alkaline Ca2+-chelating conditions, a procedure which is considered to disrupt the functional association of a Ca2+-cardiolipin complex with the enzyme, it is suggested that cardiolipin mediates the energy transfer between enzyme subunits, thereby modulating the kinetic properties of the lipoprotein. |
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