Binding of a solubilized membrane ATPase to phospholipid bilayers

Redwood, William R.; Patel, B. K.

doi:10.1016/0005-2736(74)90007-8

Cited by 14 publications

(7 citation statements)

References 42 publications

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“…The apparent change in entropy is +2J K-1 molh'. The results contrast with the change in apparent association constant with temperature reported for the binding of a solubilized membrane adenosine triphosphatase to phospholipid bilayers (Redwood & Patel, 1974). For this enzyme, the apparent association constant did not significantly change with temperature.…”

Section: Discussioncontrasting

confidence: 97%

Adsorption of glyceraldehyde 3-phosphate dehydrogenase on condensed monolayers of phospholipid

Wooster¹,

Wrigglesworth²

1976

Biochemical Journal

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The adsorption of [14C] alkylated glyceraldehyde 3-phosphate dehydrogenase from rabbit muscle to condensed monolayers of phosphatidic acid was investigated under a variety of conditions. 2. The rate constant for association at 20 degrees C depended on ionic strength. At I/2=60mM the rate constant was 0.39min-1. At I/2=260mM it decreased to 0.27min-1. 3. The apparent association constant (Kass.) for adsorption at I/2=60mM was 1.06 X 10(6)M-1 and was strongly influenced by subphase changes in pH and ionic strength. Measurements of Kass. at 20 degrees and 5 degrees C gave a value for the apparent enthalpy change on adsorption of -33kJ-mol-1. Calculations of the apparent change in free energy and apparent entropy change for the adsorption process gave values of -34kJ-mol-1 and +2J-K-1-mol-1 respectively. 4. Decreasing the amount of phosphatidic acid in the monolayer by replacement with phosphatidylcholine caused the shape of the adsorption isotherm to change from apparent hyperbolic to sigmoid. Subphase changes in pH or ionic strength did not affect the shape of the adsorption isotherm. However, adsorption of enzyme on monolayers of 100% phosphatidic acid in the presence of 1mM-CaCl2 was sigmoid in nature. 5. It is concluded that glyceraldehyde 3-phosphate dehydrogenase binds to condensed charged monolayers by multiple electrostatic interactions. At low concentrations of phosphatidic acid in the monolayer or in the presence of Ca2+, this occurs in a two-step process and depends on lateral diffusion of phosphatidic acid for strong binding to take place.

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Section: Discussioncontrasting

confidence: 97%

Adsorption of glyceraldehyde 3-phosphate dehydrogenase on condensed monolayers of phospholipid

Wooster¹,

Wrigglesworth²

1976

Biochemical Journal

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“…Binding studies. The method used was based on that of Redwood & Patel (1974). Liposomes were prepared as described above and 1 ml samples (approx.…”

Section: Methodsmentioning

confidence: 99%

“…The phospholipid 1,2-dimyristoyl-sn-glycero-3phosphocholine has been reported to undergo a phase transition at about 24°C (Redwood & Patel, 1974), and the transition temperature found for the activity of acetylcholinesterase bound to liposomes composed of this phospholipid and myristic acid was in the same range, at approx. 21°C (Fig.…”

Section: Effect Ofliposomes On the Km Ofacetylcholinesterasementioning

confidence: 97%

“…This large positive entropy change after the adsorption of acetylcholinesterase to liposomes suggests that the association is predominantly hydrophobic (Kauzmann, 1959;Schachman, 1963). Redwood & Patel (1974) also obtained a large entropy change when studying the binding of adenosine triphosphatase to liposomes and interpreted this as indicating that the interaction between the lipid and protein molecules was hydrophobic in nature. For brain acetylcholinesterase, the presence of predominantly hydrophobic binding would support the idea that the enzyme is an integral protein interacting with the apolar interior of membranes in vivo, an idea supported by the necessity to use detergents to bring the enzyme into solution (Jackson & Aprison, 1966;Ho & Ellman, 1969;McIntosh & Plummer, 1973).…”

Section: Effect Ofliposomes On the Km Ofacetylcholinesterasementioning

confidence: 97%

“…Acetylcholinesterase and liposomes of 50% 1,2dimyristoyl -sn -glycero -3 -phosphocholine and 50% myristic acid Temperature andenzyme activity. The phospholipid 1 ,2-dimyristoyl-sn-glycero-3-phosphocholine shows a phase change at 24°C (Redwood & Patel, 1974). Table 1.…”

Section: Effect Ofliposomes On the Km Ofacetylcholinesterasementioning

confidence: 99%

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The interaction of purified acetylcholinesterase from pig brain with liposomes

Reavill¹,

Wooster²,

Plummer³

1978

Biochemical Journal

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The binding of pig brain acetylcholinesterase to artificial phospholipid membranes was investigated at different temperatures. Calculation of the thermodynamic parameters revealed a small negative enthalpy change, but a large negative change in the free energy and a large positive change in the entropy on binding. The large entropy change might be interpreted as being responsible for forming the enzyme-membrane complex and was indicative of hydrophobic interactions between lipid and protein. This conclusion would also favour the hypothesis that the enzyme was an integral protein. Further support for this theory was provided by the study of acetylcholinesterase binding to liposomes containing the phospholipid 1,2-dimyristoyl-sn-glycero-3-phosphocholine. Lowering the temperature below the transition temperature or incorporating cholesterol into the liposomes decreased enzyme binding. Both factors could be interpreted as decreasing the fluidity of the hydrocarbon side chains of the phospholipids, causing an increase in bilayer thickness due to closer packing of side chains. This membrane condensation would certainly not favour the binding of integral protein molecules.

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Reconstituted Membrane Systems

Wrigglesworth¹

1984

Membrane Processes

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Binding of a solubilized membrane ATPase to phospholipid bilayers

Cited by 14 publications

References 42 publications

Adsorption of glyceraldehyde 3-phosphate dehydrogenase on condensed monolayers of phospholipid

Adsorption of glyceraldehyde 3-phosphate dehydrogenase on condensed monolayers of phospholipid

The interaction of purified acetylcholinesterase from pig brain with liposomes

Reconstituted Membrane Systems

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