Alfar Nicksch
Max Planck Society
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Featured researches published by Alfar Nicksch.
Biochimica et Biophysica Acta | 1983
Jürgen Stümpel; Hansjörg Eibl; Alfar Nicksch
The effect of variation of the acyl chain composition of phosphatidylcholines upon thermal behaviour of multilamellar liposomes was evaluated by calorimetry and X-ray studies. A total of thirteen different phosphatidylcholines were examined. They differed from each other in the length as well as in the position of the acyl chains in the glycerol backbone. The experimental results show that the hitherto accepted phase scheme for phosphatidylcholine-water systems is incomplete and has to be extended to include the behaviour of samples that have been stored for long times at low temperatures. The X-ray results show that the structure of the new low-temperature phase is not in agreement with the hexagonal packing of the acyl chains. To explain the X-ray results, a two-dimensional orthorhombic unit cell has to be assumed in order to fit all the observed reflexes in the wide-angle region.
Chemistry and Physics of Lipids | 1978
Hansjörg Eibl; Alfar Nicksch
Abstract The bromoethylesters of phosphatidic acids and their analogues are general intermediates in the synthesis of phospholipids. A direct amination with different amines such as ammonia, methylamine, dimethylamine and trimethylamine results in the corresponding phosphatidylethanolamines and -cholines. In addition to the well elaborated reactions of bromoethylesters with trimethylamine and dimethylamine, the synthesis of phosphatidylethanolamines and -( N -methyl)-ethanolamines by amination with ammonia and methylamine is now possible in high yields (> 90%) without the need of the usual protecting groups.
Analytical Biochemistry | 1977
Winchil L. C. Vaz; Konrad Kaufmann; Alfar Nicksch
Abstract A method is described for the rapid and quantitative assay of the association of proteins with lipid membranes. The method utilizes the nonradiative transfer of energy between fluorescent groups in the protein and fluorescent groups attached to the polar heads of the lipids in the membrane. The association constant for the electrostatic association of trypsin with bilayers of the negatively charged lipid, 1,2-dimyristoyl- sn -glycerol-3-phosphoric acid methyl ester (MPA) at a salt concentration of 5 m m and pH 8 was found to be (2.32 ± 0.07) × 10 5 m −1 . The stoichiometry of lipid to protein in the association complex is 40–50 lipid molecules per trypsin molecule. Honey-bee venom melittin and the serum apolipoprotein, apo-Lp-Ala, were shown to associate with lecithin vesicles. Acetylcholine esterase isolated from the electric organ of the electric eel according to the method of Leuzinger and Baker [(1967) Proc. Nat. Acad. Sci. USA 57, 446–451] was shown to be incapable of associating with lecithin or MPA bilayers.
FEBS Journal | 1978
Winchil L. C. Vaz; Alfar Nicksch; Fritz Jähnig
Archive | 1981
Hansjörg Eibl; Alfar Nicksch
Archive | 1977
Hansjörg Eibl; Alfar Nicksch
Archive | 1974
Hansjörg Eibl; Alfar Nicksch
Archive | 1981
Hansjörg Eibl; Alfar Nicksch
Archive | 1974
Hansjörg Eibl; Alfar Nicksch
European Biophysics Journal | 1980
Jrgen Stmpel; Alfar Nicksch; Hansjrg Eibl