title: The effects of hydrostatic pressure on the conformation of plasminogen.
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.
authors.affiliation: Enzyme Research Group, Department of Chemistry and Biochemistry, Concordia University, Montreal, Quebec, Canada. jkrnbltt@vax2.concordia.ca
authors.forename: J A
authors.initials: JA
authors.lastname: Kornblatt
authors.forename: M J
authors.initials: MJ
authors.lastname: Kornblatt
authors.forename: C
authors.initials: C
authors.lastname: Clery
authors.forename: C
authors.initials: C
authors.lastname: Balny
mesh_terms: D015119:Aminocaproic Acid / Q000494:pharmacology; D000818:Animals; D000933:Antifibrinolytic Agents / Q000494:pharmacology; D004285:Dogs; D006874:Hydrostatic Pressure; D010958:Plasminogen / Q000737:chemistry* / Q000187:drug effects; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D013499:Surface Properties; D017186:Titrimetry; D014867:Water / Q000737:chemistry
chemical_list: D000933:Antifibrinolytic Agents; D014867:Water; D010958:Plasminogen; D015119:Aminocaproic Acid