Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles
- 1 December 1976
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 159 (3) , 627-631
- https://doi.org/10.1042/bj1590627
Abstract
1. The adsorption of [14C]carboxymethylated glyceraldehyde 3-phosphate dehydrogenase to negatively charged liposomes of phsphatidic acid/phosphatidylcholine (3:7, w/w) was investigated. The apparent association constant at I/2 = 60, pH 7.6, was 0.4 × 10(6)M-1. Adsorption decreased as ionic strength and pH were increased. 2. In the presence of negatively charged liposomes, the Km value for glyceraldehyde 3-phosphate of glyceraldehyde 3-phosphate dehydrogenase was increased and Vmax. decreased. In the presence of positively charged liposomes, the Km value for glyceraldehyde 3-phosphate decreased and there was no significant change in Vmax. Addition of Triton X-100 abolished the effect of both positively and negatively charged liposomes on the kinetic properties of the enzyme.This publication has 17 references indexed in Scilit:
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