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Biomedical subjects

A D Albert

Publications and source records attributed to A D Albert.

44 records · Page 3Linked to original sources
PubMed1984

Perturbations of phospholipid head groups by membrane proteins in biological membranes and recombinants.

P-31 nuclear magnetic resonance (NMR) spin-lattice relaxation times (T1) have been used to probe the behavior of phospholipid head groups in the presence of membrane proteins. Measurements have been made on rabbit muscle sarcoplasmic reticulum and recombinants of the Ca2+ Mg2+ ATPase, rod outer segment disk membranes and recombinants of rhodopsin, and human erythrocyte ghosts and recombinants of human erythrocyte glycophorin. Recombined membranes with lipid/protein ratios greater than or equal to that found in biological membranes showed T1 behavior similar to the biological membranes and pure phosphatidylcholine. However, recombined membranes with a low lipid/protein ratio exhibited a T1 that was dramatically shorter than any of the other systems. Analysis of the relaxation mechanism and the factors contributing to it implicate a phospholipid head group conformation change at high protein content. It is suggested that this is due to trapping of phospholipid between proteins and is not the same phenomenon as motional restriction at the lipid-protein interface at higher lipid contents.

Animals↗
PubMed1983

Phospholipid domains in bovine retinal rod outer segment disk membranes.

Phospholipid behavior in bovine retinal rod outer segment disk membranes and in phosphatidylcholine membranes containing the photopigment rhodopsin is explored. 31P NMR spectra of these systems show two distinguishable resonances. One resembles closely the 31P NMR resonance normally obtained from phospholipid bilayers. The other resonance is much broader. Thus, there appear to be two phospholipid head-group domains in this retinal membrane. Each environment confers different properties on the head groups. Phosphatidylcholine membranes containing the disk photopigment also show two phospholipid domains. Therefore, the environment in the retinal rod outer segment disk membranes characterized by the broad resonance may arise from the influence of the integral membrane protein rhodopsin on the membrane phospholipid bilayer.

Animals↗
PubMed1982

Solubilization of phosphatidylcholine bilayers by octyl glucoside.

The solubilization of large, unilamellar egg phosphatidylcholine vesicles by the nonionic detergent octyl glucoside (OG) was investigated by nuclear magnetic resonance (NMR), fluorescence anisotropy, turbidity, electron microscopy, and centrifugation followed by compositional analysis. The solubilization process is well described by the three-stage model previously proposed for other detergents. In stage I, the OG partitions between the bilayer and aqueous phases with a molar partition coefficient of 59 +/- 6. The presence of OG in the bilayers produces a small "fluidizing" effect, as indicated by changes in the NMR and fluorescence anisotropy parameters. A rearrangement that forms large mixed bilayers occurs in the latter part of stage I. Stage II, the conversion of detergent-saturated bilayers into mixed micelles, begins at a ratio of total OG concentration minus the critical micelle concentration to total phosphatidylcholine concentration of approximately 1.5 and continues until this ratio reaches about 3.0. The correction for the critical micelle concentration of the OG is necessary for comparison of experimental results obtained at different lipid concentrations. The mixed bilayer-mixed micelle interconversion is quantified by the centrifugation experiments and by 31P NMR. The agreement between the two methods is excellent. Advantages of the NMR method are discussed. In stage III, which was not studied in detail here, all of the phosphatidylcholine is present as mixed micelles. Evidence is presented that the various structures present in the dispersions are in equilibrium with one another during these experiments.

Fluorescence Polarization↗
PubMed1982

The extent of transmembrane phospholipid movement in mixed phosphatidylcholine-phosphatidylserine vesicles.

A hypothesis of rapid coupled translocation of egg phosphatidylcholine and bovine brain phosphatidylserine across a mixed vesicle membrane was tested. Homogeneous preparations of sonicated phospholipid vesicles containing four different compositions of the above two phospholipids were prepared. Trinitrobenzene-sulfonate derivatization of vesicle-phosphatidylserine was used to determine the outside-inside ratio of this phospholipid. No change in the ratio was observed over a 2-hr period. The transmembrane distribution of phosphatidylcholine was quantitated using 600 MHz 1H NMR; this distribution was found to be identical after a 24-hr incubation at pH 5 or pH 8. Thus, rapid exchange of phosphatidylcholine for phosphatidylserine is not observed under the conditions of these experiments.

Kinetics↗
PubMed1981

Evidence for the influence of the protein-phospholipid interface on sarcoplasmic reticulum Ca++ Mg++ ATPase activity.

Sarcoplasmic reticulum from the white hind leg muscle of the rabbit was examined with 31P nuclear magnetic resonance as a nonperturbing probe of phospholipid-protein interactions in the intact membrane. The phospholipids of the sarcoplasmic reticulum appear to inhabit two distinct environments: one very similar in behavior to pure phospholipid lamellar dispersions and the other immobilized by the protein in the membrane. Measurement of the population of the latter environment suggests that it is dependent on salt concentration and probably not due to the Ca++ Mg++ ATPase of the sarcoplasmic reticulum. This immobilization can be removed completely by papain proteolysis of the membrane protein, but only partially by trypsin treatment. The phospholipid composition of recombinants with the Ca++ Mg++ ATPase was varied in order to look for effects of the phospholipid-protein interface on enzymatic activity of the Ca++ Mg++ ATPase. Both transphosphatidylated phosphatidylethanolamine (from egg phosphatidylcholine) and bovine brain phosphatidylserine readily partitioned into the putative boundary layer, whereas under the same conditions soybean phosphatidylethanolamine was excluded. Only phosphatidylserine affected the activity of the enzyme, causing an inhibition that was proportional to the phosphatidylserine content, relative to phosphatidylcholine.

Animals↗