Vanadium inhibition of serine and cysteine proteases. |
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| Authors: | N Guerrieri P Cerletti M De Vincentiis A Salvati S Scippa |
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| Affiliation: | Dipartimento di Scienze Molecolari Agroalimentari, Facoltà di Agraria, Università degli Studi di Milano, Italy. guerrier@imiucca.csi.unimi.it |
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| Abstract: | A study was made on the effect of vanadium, in both the tetravalent state in vanadyl sulphate and in the pentavalent state in sodium meta-vanadate, and ortho-vanadate, on the proteolysis of azocasein by two serine proteases, trypsin and subtilisin and two cysteine proteases bromelain and papain. Also the proteolysis of bovine azoalbumin by serine proteases was considered. An inhibitory effect was present in all cases, except meta-vanadate with subtilisin. The oxidation level of vanadium by itself did not determine the inhibition kinetics, which also depended on the type and composition of the vanadium containing molecule and on the enzyme assayed. The pattern of inhibition was similar for proteases belonging to the same class. The highest inhibition was obtained with meta-vanadate on papain and with vanadyl sulphate on bromelain. |
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