Zapun, A. and Creighton, T.E. and Rowling, P.J.E. and Freedman, R.B. (1992) Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum. Proteins-Structure Function and Genetics, 14 (1). pp. 10-15. ISSN 0887-3585.
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The rates of folding and disulfide bond formation in reduced BPTI were measured in vitro in the presence and absence of total protein from the endoplasmic reticulum. The rates were increased substantially by the endoplasmic reticulum proteins, but only to the extent expected from the known content and activity of protein-disulfide-isomerase. No effects of added ATP or Ca2+ were observed, even though protein-disulfide-isomerase binds Ca2+ tightly.
|Uncontrolled keywords:||protein disulfide isomerase; disulfide bonds; protein folding; chaperones|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||O.O. Odanye|
|Date Deposited:||27 Jul 2009 17:12|
|Last Modified:||30 May 2012 10:53|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/22291 (The current URI for this page, for reference purposes)|
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