Interaction of a solubilized membrane ATPase with lipid bilayer membranes

Redwood, William R.; Gibbes, D.C.; Thompson, T. E.

doi:10.1016/0005-2736(73)90331-3

Cited by 22 publications

(4 citation statements)

References 24 publications

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“…It is likely but not yet proved that the increase in steady state conductance produced by glycophorin in bilayers is entirely due to the formation of these channels. Thus, glycophorin is one of a growing family of proteins known to produce channel formation in bilayers, such as EIM [4,8], hemocyanin [2], black widow toxin [12], and bacterial ATPase [22].…”

Section: Discussionmentioning

confidence: 99%

Interactions between a membrane sialoglycoprotein and planar lipid bilayers

Tosteson

1978

J. Membrain Biol.

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Summary. Bilayer membranes formed from lipids dissolved in decane were exposed to glycophorin, a sialoglycoprotein which had been extracted from human red cell membranes. The interaction with the bilayer produced an increase in the steady state electrical conductance of the membrane proportional to the amount added. Fluctuations in membrane current when the electrical potential difference was constant were observed concommitantly with this increase in membrane conductance. The minimum size of the fluctuations corresponds to a conductance of 10 -1~ mho. The increase in conductance as well as the current fluctuations persisted after extensive washout of the chamber containing the protein (cisside). Subsequent addition of lcctins (wheat germ agglutinin and phytohemoagglutinin) to the cis-side produced rupture of the membranes, whilst these hemoagglutinins added to the trans-side failed to produce an effect. Measurements of changes in surface potential using K + nonactin as a probe indicated that glycophorin induces a negative surface charge. At high protein concentrations, the magnitude of the induced surface potential became independent of glycophorin concentration. The maximum number of charges introduced onto the membrane under these conditions was lax 105/gm 2. Cis (but not trans)-side addition of neuraminidase abolished these charges, indicating that they can be ascribed to the sialic acid residues that the protein bears. These results suggest that glycophorin incorporates into bilayer membranes with its N-terminal end (where the sialic acid and carbohydrates are located) facing the cis-side. Spectrin reversibly lowered the glycophorininduced membrane conductance when added to the trans-side. Cis-side additions failed to produce an effect. Trypsin present on the trans-side irreversibly lowered the membrane conductance. These results indicate that parts of the glycophorin molecule, probably the C-terminal end, are accessible to reagents in the solution bathing the trans-side of the membrane. Thus glycophorin spans the planar bilayer in much the same way as it spans the red cell membrane.During recent years, investigations in many laboratories have been directed toward illuminating the relationship between function and molecular architecture of biological membranes. The concept has emerged

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Section: Discussionmentioning

confidence: 99%

Interactions between a membrane sialoglycoprotein and planar lipid bilayers

Tosteson

1978

J. Membrain Biol.

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“…Similar conclusions have also been drawn from the results of analogous experiments using bacterial membranes which, as a result of genetic manipulation, have been depleted of F1 or contain structurally defective of F1 or F0 components (see below). In this respect, it is interesting to note that the addition of purified F1 from S. faecalis to artificial phospholipid bilayers causes a large increase in electrical conductance, which is claimed to be compatible with the formation of discrete, but relatively wide, aqueous-filled channels (327).…”

Section: Cytoplasmmentioning

confidence: 99%

Bacterial respiration.

Haddock¹,

Jones²

1977

Bacteriological Reviews

392

205

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“…Conductance with proteins (such as cytochrome oxidase and bacteriorhodopsin) is possible when they are incorporated into liposomes fused to a black lipid membrane [55–57]. Such conductance has also been demonstrated for Na + /K + ‐ATPase and H + ‐ATPase [57–59]. The light‐driven production of ATP is catalysed by chloroplast F 0 F 1 ‐ATP synthase in an artificial photosynthetic membrane, albeit in a non‐uniform orientation [47].…”

Section: Discussionmentioning

confidence: 99%

Uniformly oriented bacterial F₀F₁‐ATPase immobilized on a semi‐permeable membrane: a step towards biotechnological energy transduction

Bhattacharya¹,

Schiavone²,

Nayak³

et al. 2004

Biotech and App Biochem

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The immobilization of F(0)F(1)-ATPase in uniform orientation is reported. The biotinylated and histidine-tagged subunits of the bacterial F(0)F(1)-ATPase complex were used for immobilization of the complex on artificial semi-permeable membranes resulting in 88+/-7.8 and 72+/-5.2% coupling of the enzymes. The immobilized enzymes retained over 90% activity. The immobilized ATPase/synthase was used for generation of ATP from ADP and P(i) at the expense of electrochemical potential energy. The re-usability, ratio of amount of enzyme immobilized to enzymic activity conferred on the membranes, ATP synthesized by assembled system and suitability of ATP generated for use in coupled enzymic reactions were determined.

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Interaction of a solubilized membrane ATPase with lipid bilayer membranes

Cited by 22 publications

References 24 publications

Interactions between a membrane sialoglycoprotein and planar lipid bilayers

Interactions between a membrane sialoglycoprotein and planar lipid bilayers

Bacterial respiration.

Uniformly oriented bacterial F₀F₁‐ATPase immobilized on a semi‐permeable membrane: a step towards biotechnological energy transduction

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Interaction of a solubilized membrane ATPase with lipid bilayer membranes

Cited by 22 publications

References 24 publications

Interactions between a membrane sialoglycoprotein and planar lipid bilayers

Interactions between a membrane sialoglycoprotein and planar lipid bilayers

Bacterial respiration.

Uniformly oriented bacterial F0F1‐ATPase immobilized on a semi‐permeable membrane: a step towards biotechnological energy transduction

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Uniformly oriented bacterial F₀F₁‐ATPase immobilized on a semi‐permeable membrane: a step towards biotechnological energy transduction