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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