Influence of temperature on the conformation of canine plasminogen: An analytical ultracentrifugation and dynamic light scattering study
		
		
		
			
Influence of temperature on the conformation of canine plasminogen: An analytical ultracentrifugation and dynamic light scattering study
Engineering Village 2
2006 Elsevier Inc
Accession number:  05409402245 
 
 Title:  Influence of temperature on the conformation of canine plasminogen: An analytical ultracentrifugation and dynamic light scattering study 
 
 Authors:  Kornblatt, Jack A.; Schuck, Peter  
 
 Author affiliation:  Enzyme Research Group, Department of Biology, Concordia University, Montreal, Que. H4B 1R6, Canada 
 
 Serial title:  Biochemistry 
 
 Abbreviated serial title:  Biochemistry 
 
 Volume:  v 44 
 
 Issue:  n 39 
 
 Issue date:  Oct 4 2005 
 
 Publication year:  2005 
 
 Pages:  p 13122-13131 
 
 Language:  English 
 
 ISSN:  0006-2960 
 
 CODEN:  BICHAW 
 
 Document type:  Journal article (JA) 
 
 Publisher:  American Chemical Society, Columbus, OH 43210-3337, United States 
 
 Abstract:  Plasminogen is known to undergo an extremely large conformational change when it binds ligands; the two well-established conformations are either closed (absence of external ligand) or open (presence of external ligand). We show here that plasminogen is more complicated than can be accommodated by a two-state, closed/open, model. Temperature changes induce large structural changes which can be detected with either dynamic light scattering or analytical ultracentrifugation. The temperature-induced changes are not related to the classical closed/open conformational change since both closed and open forms of the protein are similarly influenced. It appears as though the packing density of the protein increases as the temperature is raised. Over the range 4-20 ?C, the Stokes' radius of the classical closed plasminogen goes from 4.7 to 4.2 nm, and that of the classical open form goes from 5.55 to 5.0 nm. These changes in packing can be rationalized if temperature change induces a large conformational change and if this is accompanied by a large change in hydration, by a change in solute binding, or by a change in the total void volume of the protein. ? 2005 American Chemical Society. 
 
 Number of references:  43 
 
 Ei main heading:  Animal cell culture 
 
 Ei controlled terms:  Conformations  -  Temperature distribution  -  Light scattering  -  Binding energy 
 
 Uncontrolled terms:  Canine plasminogen  -  Ligands  -  Ultracentrifugation 
 
 Ei classification codes:  461.2 Biological Materials  -  801.4 Physical Chemistry  -  641.1 Thermodynamics  -  741.1 Light/Optics 
 
 Treatment:  Experimental (EXP) 
 
 DOI:  10.1021/bi050895y 
 
 Database:  Compendex 
 
   Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved 
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