Conformational changes of bovine β-trypsin and trypsinogen induced by divalent ions: An energy-dispersive X-ray diffraction and functional study
The radius of gyration ( R g) of bovine trypsinogen and β-trypsin was measured by an energy-dispersive X-ray technique as a function of Ca 2+ or SO 4 2− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca 2+ to its binding site(s) on both...
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Veröffentlicht in: | Archives of biochemistry and biophysics 2006-05, Vol.449 (1), p.157-163 |
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Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The radius of gyration (
R
g) of bovine trypsinogen and β-trypsin was measured by an energy-dispersive X-ray technique as a function of Ca
2+ or SO
4
2− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca
2+ to its binding site(s) on both serine proteases and some of their adducts (with an effector and/or an inhibitor). As a whole, all information reported in the present work demonstrates that: (i) the strains exerted by different ions on these proteases produce diverse structural modifications; and (ii) at least in the case of Ca
2+, the changes in
R
g can be ascribed to the direct interaction of the binding site(s) on the protein matrix with the cation. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/j.abb.2006.02.010 |