Craubner H et al. 1975
- Authors:
Craubner H. Koenig F. Schmid GH.
- Title:
Determination of the molecular weight and the hydrodynamic properties of a
polypeptide from the thylakoid membrane by sedimentation, diffusion and
binding measurements in dodecyl sulphate solutions.
- Reference location:
Zeitschrift fur Naturforschung - Section C - Biosciences. 30(5):615-21,
1975 Sep-Oct.
- Abstract:
The molecular weight and hydrodynamic properties of a polypeptide isolated
from the lamellar system of Antirrhinum chloroplasts were determined in
sodium dodecyl sulphate solution by measurement of sedimentation velocity,
diffusion and effective partial specific volume. The polypeptide fraction
exhibits a molecular weight of 25000 which agrees with the apparent
molecular weight found by polyacrylamide gel electrophoresis. The
molecular weight of the polypeptide-sodium dodecyl sulphate micelle was 54
000, with a friction ratio of 1.6 which indicates an effective asymmetric
hydrodynamic shape. For binding measurements self-diffusion equilibrium
dialysis with dodecyl [35S] sulphate was used. In this case, dialysis
equilibrium was reached within about 10 hours, in contrast to the dialysis
with initial concentration differences which requires much longer times. A
binding value of deltaD=1.15 g sodium dodecyl sulphate per g polypeptide
was obtained which corresponds to a molar binding ratio of 100 mol dodecyl
sulphate bound per mol of polypeptide. After the removal of dodecyl
sulphate the polypeptide is present in an aggregated state. In phosphate
buffers of pH 6.8 and 7.5 the aggregates preponderantly have sedimentation
coefficients of 11.7 and 6.8 Svedberg units respectively. Assuming
equivalent spheres the molecular weights were calculated to be 340 000 and
150 000.
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