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Protein folding in the secretory pathway of animal cells

Freedman, Robert B., Greenall, Carole, Jenkins, Nigel, Tuite, Mick F. (1995) Protein folding in the secretory pathway of animal cells. Cytotechnology, 18 (1-2). pp. 77-82. ISSN 0920-9069. E-ISSN 1573-0778. (doi:10.1007/BF00744322) (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)

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. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1007/BF00744322

Abstract

The exit of newly-synthesized proteins from the lumen of the endoplasmic reticulum (ER) is the rate-determining step in protein secretion. Only correctly-folded and fully-assembled proteins exit the ER and progress along the secretory pathway. Folding and assembly in the ER are mediated by a variety of factors including folding catalysts and molecular chaperones. The properties of these factors, and the nature of their interactions with folding substrates, are beginning to be clarified. Little work has been done to characterize these processes and these factors in cell lines employed for large-scale cell culture. Manipulation of these process may permit improvement in yield or productivity of recombinant proteins by cultured animal cells.

Item Type: Article
DOI/Identification number: 10.1007/BF00744322
Uncontrolled keywords: protein folding; endoplasmic reticulum; glycosylation; disulphide bond formation; folding catalysts; chaperones; protein disulphide-isomerase
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: P. Ogbuji
Date Deposited: 01 Jun 2009 16:48 UTC
Last Modified: 06 Aug 2019 11:16 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/19534 (The current URI for this page, for reference purposes)
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