The prominent 28 kDa polypeptide in clathrin coated vesicle fractions from developing pea cotyledons is contaminating ferritin
Article first published online: 2 JAN 2013
© The Author(s) Journal compilation © 1993 International Federation for Cell Biology
Cell Biology International
Volume 17, Issue 6, pages 551–557, June 1993
How to Cite
Hoh, B. and Robinson, D. G. (1993), The prominent 28 kDa polypeptide in clathrin coated vesicle fractions from developing pea cotyledons is contaminating ferritin. Cell Biology International, 17: 551–557. doi: 10.1006/cbir.1993.1098
- Issue published online: 2 JAN 2013
- Article first published online: 2 JAN 2013
- Paper received 23.02.93. Revised paper accepted 12.03.93.
- Cited By
SDS-PAGE of clathrin coated vesicle (CCV) fractions prepared from developing pea cotyledons are characterized by the presence of a 28 kDa polypeptide. Like clathrin light chains, this polypeptide is heat-stable and can bind calcium ions. However, the distribution of this polypeptide is not identical to that of clathrin in the rate zonal gradients used to purify CCV. Negatively stained preparations reveal small, 12 nm diameter hollow particles, in addition to CCV. As judged by the electron dense centre to these particles, we infer that CCV preparations from pea cotyledons are contaminated with phytoferritin. This has been confirmed by immuno-blotting with pea ferritin antibodies. The degree of phytoferritin contamination in CCV fractions is greater when RNase digestion of postmicrosomal pellets is performed at cold, rather than warm temperatures.