Bose, S. and Freedman, Robert 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 currently available from this repository. You may be able to access a copy if URLs are provided)
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.
|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:||16 Jun 2014 14:17|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/20394 (The current URI for this page, for reference purposes)|