Modification of Glyceraldehyde 3-Phosphate Dehydrogenase Activity by Adsorption to Erythrocyte Membranes and Phospholipid Vesicles

Wrigglesworth, John M.; Keokitichai, Sindhchai; Wooster, M S; Millar, Fiona A.

doi:10.1042/bst0040637

Cited by 8 publications

(2 citation statements)

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“…The activity of glyceraldehyde 3-phosphate dehydrogenase was monitored at 200C by following the reduction of NAD+ at 340 nm by using a Perkin-Elmer SP356 dual-wavelength spectrophotometer in its dual-wavelength mode with a reference wavelength of 370nm. The conditions of assay were as previously described (Wrigglesworth et al, 1976). Lactate dehydrogenase was assayed as described by Gay et al (1968).…”

Section: Methodsmentioning

confidence: 99%

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

Keokitichai¹,

Wrigglesworth²

1980

Biochemical Journal

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Intact human erythrocytes were exposed to low concentrations of glutaraldehyde. After washing and subsequent lysis of the cells, glyceraldehyde 3-phosphate dehydrogenase activity is found to be associated with a membrane fraction and cannot be eluted by salt treatment. Lactate dehydrogenase activity is associated with a supernatant fraction under the same conditions. Preincubation of the intact cells under conditions designed to increase internal NADH concentrations, leads to a lower membrane-associated activity of glyceraldehyde 3-phosphate dehydrogenase after lysis.

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Section: Methodsmentioning

confidence: 99%

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

Keokitichai¹,

Wrigglesworth²

1980

Biochemical Journal

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“…The adsorption of the enzyme to the inner surface of the erythrocyte membrane is sensitive to micromolar concentrations of its substrates as well as to the ionic strength of the suspending medium (Kant & Steck, 1973). Preliminary results reported by Wrigglesworth et al (1976) suggest that when glyceraldehyde 3-phosphate dehydrogenase is adsorbed to the inner surface of the erythrocyte membrane, the kinetic properties of the enzyme ae-modified. The possibility arises that attachment of the enzyme to the membrane in vivo and the subsequent modiction of the activity ofthre enzyme are regulated by changes in substrate centrations.…”

Section: Discussionmentioning

confidence: 99%

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

Wooster¹,

Wrigglesworth²

1976

Biochemical Journal

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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.

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Dehydrogenases of the Plasma Membrane

Crane

Goldenberg

Morré

et al. 1979

Subcellular Biochemistry

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Modification of Glyceraldehyde 3-Phosphate Dehydrogenase Activity by Adsorption to Erythrocyte Membranes and Phospholipid Vesicles

Cited by 8 publications

References 0 publications

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

Association of glyceraldehyde 3-phosphate dehydrogenase with the membrane of the intact human erythrocyte

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

Dehydrogenases of the Plasma Membrane

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