Activation of glucose diffusion from egg lecithin liquid crystals by serum albumin.
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Summary
At acid pH, bovine serum albumin enhances the rate at which glucose diffuses from lecithin-cholesterol-dicetyl phosphate micelles, which is close to the pH at which the well-known acid conformation change occurs in this protein.
- Type
- article
- Published
- 1969-01-28
- Cited by
- 48
- References
- 15
- OpenAlex
- https://openalex.org/W5813302
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12725028
Keywords
Conjunction (astronomy), Scale (ratio), Identity (music), Psychology, Linguistics
References
- Chromatographically homogeneous lecithin from egg phospholipids
- Changes in optical rotation in the acid transformations of plasma albumin. Evidence for the contribution of tertiary structure to rotatory behavior.
- FRAGMENTATION OF BOVINE SERUM ALBUMIN BY PEPSIN. I. THE ORIGIN OF THE ACID EXPANSION OF THE ALBUMIN MOLECULE.
- Removal of fatty acids from serum albumin by charcoal treatment.
- NEGATIVE STAINING OF PHOSPHOLIPIDS AND THEIR STRUCTURAL MODIFICATION BY SURFACE-ACTIVE AGENTS AS OBSERVED IN THE ELECTRON MICROSCOPE.
- Phospholipid model membranes. II. Permeability properties of hydrated liquid crystals.
- Electrophoretic Behavior of Bovine Plasma Albumin At Low pH
- HYDROPHOBIC INTERACTIONS IN PROTEINS: CONFORMATION CHANGES IN BOVINE SERUM ALBUMIN BELOW PH5.
- Staphylococcal Alpha-Toxin: Effects on Artificial Lipid Spherules
- The action of steroids and streptolysin S on the permeability of phospholipid structures to cations.
- A contribution to the theory of permeability of thin films
- Diffusion of univalent ions across the lamellae of swollen phospholipids.
- The Reversible Expansion of Bovine Serum Albumin in Acid Solutions1
- Changes in the Intrinsic Viscosity and Optical Rotation of Bovine Plasma Albumin Associated with Acid Binding1
- On The Aggregation Of Boving Serum Albumin In Acid pH
Cited by
- Light-scattering measurement of lipid-glycoprotein interaction
- Biomembranen: Struktur und Funktion
- Effects of poly(ethylene glycol) on liposomes and erythrocytes. Permeability changes and membrane fusion.
- The interaction of human serum albumin and model membranes.
- Binding and aggregate formation of phospholipid liposomes containing phosphatidic acid with ovalbumin.
- Protein-lipid interactions.
- Interaction of the erythrocyte--membrane protein, spectrin, with model membrane systems.
- Phospholipid-protein interactions: membrane permeability correlated with monolayer "penetration".
- Dynamic Mechanical Spectroscopy of Biomembrane Systems
- Model transport studies utilizing lecithin spherules IV: transport of D-glucose in spherules prepared from lecithin, dicetyl phosphate, and cholesterol.
- Structural studies by X-ray diffraction of model lipid-protein membranes of serum albumin-lecithin-cardiolipin.
- pH-sensitive liposomes: possible clinical implications.
- Synergistic effects of a membrane protein (spectrin) and Ca 2+ on the Na + permeability of phospholipid vesicles.
- The role of bovine serum albumin on the permeability of a model membrane.
- The binding of serum albumin to phospholipid liposomes.
- Measurement of the glucose permeation rate across phospholipid bilayers using small unilamellar vesicles. Effect of membrane composition and temperature.
- Structure of macromolecular aggregates. II. Construction of model membranes from phospholipids and polypeptides.
- Phospholipid vesicles (liposomes) as models for biological membranes: Their properties and interactions with cholesterol and proteins
- Estrophilic binding sites of the uterus. Relation to uptake and retention of estradiol in vitro.
- The interaction of polyamino acids with lipid monolayers.
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