Binding of glyceraldehyde-3-phosphate dehydrogenase to phospholipid liposomes
J Gutowicz, T Modrzycka - Biochimica et Biophysica Acta (BBA) …, 1978 - Elsevier
J Gutowicz, T Modrzycka
Biochimica et Biophysica Acta (BBA)-Biomembranes, 1978•ElsevierThe binding of glyceraldehyde-3-phosphate dehydrogenase prepared from rabbit muscle to
phospholipid model membranes (liposomes) as a function of pH, ionic strength, and the
influence of the binding on specific activity of the enzyme was studied. The binding
decreases the specific activity of the enzyme. The binding was studied by the method of
association of the enzyme with liposomes during centrifugation. The existence of a dominant
interaction of electrostatic character was found.
phospholipid model membranes (liposomes) as a function of pH, ionic strength, and the
influence of the binding on specific activity of the enzyme was studied. The binding
decreases the specific activity of the enzyme. The binding was studied by the method of
association of the enzyme with liposomes during centrifugation. The existence of a dominant
interaction of electrostatic character was found.
Abstract
The binding of glyceraldehyde-3-phosphate dehydrogenase prepared from rabbit muscle to phospholipid model membranes (liposomes) as a function of pH, ionic strength, and the influence of the binding on specific activity of the enzyme was studied. The binding decreases the specific activity of the enzyme. The binding was studied by the method of association of the enzyme with liposomes during centrifugation. The existence of a dominant interaction of electrostatic character was found.
Elsevier
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