Peptidyl-Prolyl CIS-Trans-Isomerase Activity Associated with the Endoplasmic-Reticulum

Bose, S. and Freedman, R.B. (1994) Peptidyl-Prolyl CIS-Trans-Isomerase Activity Associated with the Endoplasmic-Reticulum. Biochemical Journal, 300 . pp. 865-870. ISSN 0264-6021. (The full text of this publication is not available from this repository)

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Abstract

Peptidyl prolyl cis-trans-isomerase (PPI) activity was detected in microsomal fractions from bovine and rat liver. Extensive washing, proteinase and sonication treatments indicated that although some of this activity was due to adsorbed cytosolic enzymes, there was also an active but latent microsomal PPI activity. Density-gradient subfractionation indicated that activity was associated with vesicles derived from both the rough and the smooth endoplasmic reticulum (ER), suggesting that the activity was located within the ER lumen. The luminal PPI activity was inhibited by cyclosporin A and was active towards an unfolded protein substrate as well as towards the standard peptide substrate.

Item Type: Article
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: 26 Aug 2009 20:29
Last Modified: 30 May 2012 10:54
Resource URI: http://kar.kent.ac.uk/id/eprint/20394 (The current URI for this page, for reference purposes)
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