Conformational changes of bovine beta-trypsin and trypsinogen induced by divalent ions: an energy-dispersive X-ray diffraction and functional study |
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Authors: | Caracciolo G Martelli A Boumis G Bellelli A Caminiti R Congiu-Castellano A Amiconi G |
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Affiliation: | Dipartimento di Chimica, Università di Roma La Sapienza and INFM, 00185 Roma, Italy. a.congiu@caspur.it |
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Abstract: | The radius of gyration (R(g)) of bovine trypsinogen and beta-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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