|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
Journal of Cell Science, Vol 90, Issue 3 485-491, Copyright © 1988 by Company of Biologists
JOURNAL ARTICLES |
GL Koch, DR Macer and FB Wooding
Medical Research Council Laboratory of Molecular Biology, Cambridge, England.
The location of endoplasmin in the endoplasmic reticulum was investigated by biochemical and immunoelectron microscopic analyses. The protein could be obtained in a soluble form by procedures that do not involve the use of any detergents. The soluble protein has the amino- and carboxy-terminal sequences of the intact molecule, showing that it has not been proteolysed. Application of the Triton X-114 phase-separation test does not reveal significant hydrophobicity in the molecule. Immunogold labelling studies on cells with a dilated endoplasmic reticulum (ER) lumen show that endoplasmin is uniformly distributed throughout the lumen, with no evidence of a preferential association with the membrane. These studies clearly demonstrate that endoplasmin is a luminal protein of the ER, i.e. a reticuloplasmin, and not an integral membrane protein.
This article has been cited by other articles:
![]() |
J. D. Feramisco, J. L. Goldstein, and M. S. Brown Membrane Topology of Human Insig-1, a Protein Regulator of Lipid Synthesis J. Biol. Chem., February 27, 2004; 279(9): 8487 - 8496. [Abstract] [Full Text] [PDF] |
||||
![]() |
N. G. Zelenski, R. B. Rawson, M. S. Brown, and J. L. Goldstein Membrane Topology of S2P, a Protein Required for Intramembranous Cleavage of Sterol Regulatory Element-binding Proteins J. Biol. Chem., July 30, 1999; 274(31): 21973 - 21980. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Nohturfft, M. S. Brown, and J. L. Goldstein Topology of SREBP Cleavage-activating Protein, a Polytopic Membrane Protein with a Sterol-sensing Domain J. Biol. Chem., July 3, 1998; 273(27): 17243 - 17250. [Abstract] [Full Text] [PDF] |
||||