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Published on: April 1, 2015
The effects of hydrostatic pressure on the conformation of plasminogen
J A Kornblatt1, M J Kornblatt, C Clery
1Enzyme Research Group, Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, Canada. jkrnbltt@vax2.concordia.ca
Abstract:
Plasminogen undergoes a large conformational change when it binds 6-aminohexanoate. Using ultraviolet absorption spectroscopy and native PAGE, we show that hydrostatic pressure brings about the same conformational change. The volume change for this conformational change is -33 mL.mol-1. Binding of ligand and hydrostatic pressure both cause the protein to open up to expose surfaces that had previously been buried in the interior.
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