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. 1976 Dec 1;159(3):627-31.
doi: 10.1042/bj1590627.

Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles

M S Wooster, J M Wrigglesworth

Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles

M S Wooster et al. Biochem J. .

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 X 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.

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