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Influence of temperature on the conformation of canine plasminogen: an analytical ultracentrifugation and dynamic light scattering study.

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 degrees 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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Kornblatt JA,Schuck P

doi

10.1021/bi050895y

subject

Has Abstract

pub_date

2005-10-04 00:00:00

pages

13122-31

issue

39

eissn

0006-2960

issn

1520-4995

journal_volume

44

pub_type

杂志文章

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