Rowling, Pamela J. E. and McLaughlin, Stephen H. and Pollock, G.S. and Freedman, Robert B. (1994) A Single Purification Procedure for the Major Rsident Proteins of the ER Lumen - Endoplasmin,BIP,Calreticulin and Protein Disufide-Isomerase. Protein Expression and Purification, 5 (4). pp. 331-336. ISSN 1046-5928. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
We have developed a single purification procedure for the four major resident endoplasmic reticulum (ER) proteins: protein disulfide isomerase (PDI), BiP, endoplasmin, and calreticulin. Three of these proteins are thought to play a role in protein folding in vivo, whereas calreticulin is thought to be the major calcium binding protein in the ER. The proteins were purified from fresh bovine liver by taking advantage of individual characteristics of the proteins. Liver microsomes were prepared and then permeabilized to release the lumenal contents. After ammonium sulfate precipitation, the proteins were purified by chromatography; BiP was purified by affinity chromatography on ATP-agarose, and both endoplasmin and calreticulin were purified by affinity chromatography on Con A-Sepharose. PDI was purified by anionic ion exchange chromatography. (C) 1994 Academic Press, Inc.
|Subjects:||Q Science > QP Physiology (Living systems) > QP517 Biochemistry|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||P. Ogbuji|
|Date Deposited:||19 Jun 2009 09:45|
|Last Modified:||16 Jun 2014 14:16|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/20006 (The current URI for this page, for reference purposes)|