التفاصيل البيبلوغرافية
| العنوان: |
Conformational changes of bovine β-trypsin and trypsinogen induced by divalent ions: An energy-dispersive X-ray diffraction and functional study |
| المؤلفون: |
Caracciolo, G.1, Martelli, A.2, Boumis, G.3, Bellelli, A.3, Caminiti, R.1, Congiu-Castellano, A.2 a.congiu@caspur.it, Amiconi, G.3 |
| المصدر: |
Archives of Biochemistry & Biophysics. May2006, Vol. 449 Issue 1/2, p157-163. 7p. |
| مصطلحات موضوعية: |
*PANCREATIC secretions, *INTERMEDIATES (Chemistry), *PROTEOLYTIC enzymes, *SERINE proteinases |
| مستخلص: |
Abstract: 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 Ca2+ or SO4 2− concentration; these results have been supplemented with measurements of association equilibrium constants of Ca2+ 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 Ca2+, the changes in R g can be ascribed to the direct interaction of the binding site(s) on the protein matrix with the cation. [Copyright &y& Elsevier] |
| قاعدة البيانات: |
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