The Journal of Cell Biology, Vol 79, 291-313, Copyright © 1978 by The Rockefeller University Press

ARTICLES

Binding of cytochrome b5 to membranes of isolated subcellular organelles from rat liver

J Remacle

The in vitro incorporation of a well-characterized integral protein cytochrome b5 into membranes of various subcellular organelles was investigated by biochemical and immunochemical methods. Microsomes, peroxisomes, and outer mitochondrial membranes, all containing endogenous cytochrome b5, incorporated large amounts of the hemoprotein in such a way that it was reducible by an inherent NADH cytochrome b5 reductase. Lysosomal membranes did not incorporate cytochrome b5. Inner mitochondrial and Golgi membranes, which do not naturally contain cytochrome b5, bound it in vitro but it was not reduced in the presence of NADH. These results show some discrepancies between the natural localization and the in vitro binding of cytochrome b5. They confirm one aspect of the fluid membrane theory and bring new elements to our understanding of the maintenance of the specific features of the membranes of subcellular organelles with respect to the cell dynamism.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

• Hwang, Y. T., Pelitire, S. M., Henderson, M. P.A., Andrews, D. W., Dyer, J. M., Mullen, R. T. (2004). Novel Targeting Signals Mediate the Sorting of Different Isoforms of the Tail-Anchored Membrane Protein Cytochrome b5 to Either Endoplasmic Reticulum or Mitochondria. Plant Cell 16: 3002-3019 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents