The application of surface tension measurements to the study of protein-lipid interactions between a hydrophobic myelin protein (lipophilin) and lipids
✍ Scribed by Emil Katona; Dorothy Denise Wood; August Wilhelm Neumann; Mario Antony Moscarello
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 622 KB
- Volume
- 67
- Category
- Article
- ISSN
- 0021-9797
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
The lytic action of a number of N-acyl amino acids on lecithin liposomes was examined. The agents' affinity for the lecithin liposome membrane was measured and the results obtained were treated to estimate the interactions of the amino acid residues with the lecithin polar head group at the surface
Processes or interactions that can contribute to the adsorption entropy. It has been suggested 20,[22][23][24] that the major contribution to the entropy change associated with THERMODYNAMIC ANALYSIS 57
## Abstract A mechanochemical study of the process of adhesion of plasma proteins to the surface of dialysis membranes was carried out with a scanning force microscope (SFM) in the force spectroscopy mode. Three representative blood plasma proteins (fibronectin, fibrinogen, and albumin) covalently
## Abstract Co‐immunoprecipitation is the classical approach for investigating protein–protein interactions. Analysis is generally conducted using the Western blot approach. We set out to investigate whether flow cytometry was a feasible alternative to Western blotting. Using the TCR‐CD3 complex as
## Abstract Incubation of placental brush border membrane (BBM) along with sonicated vesicles of exogenous lipids (egg yolk PC) in the presence of phospholipid‐transfer protein (PL‐TP) showed a decrease in the alkaline phosphatase activity due to the change in the membrane micro‐environment, such a