The action of elastase on p-nitroanilide substrates |
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| Authors: | J Bieth C G Wermuth |
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| Affiliation: | 1. Laboratoire de Chimie, Clinique Médicale A, Hôpital Civil, 67005 Strasbourg-Cedex France.;2. Laboratoire de Chimie Organique, Faculté de Pharmacie, Université Louis Pasteur, 67083 Strasbourg-Cedex France. |
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| Abstract: | The action of elastase has been studied on four p-nitroanilides: BOC-(Ala)2-NA, (Ala)3-NA, Ac-(Ala)3-NA and BOC-(Ala)3-NA. The second order rate constant kcat/Km increases considerably with the chain length of these substrates. With (Ala)3-NA, activation by excess substrate was observed. DMF and DMSO inhibit strongly the elastase catalyzed hydrolysis of Ac- and BOC-(Ala)3-NA. The later substrate may be used to assess rapidly elastase activity: concentrations as low as 0.2 μg/ml may be determined accurately. |
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