The occurrence of a thermally induced first-order transition affecting the amidolytic activity of plasmin adsorbed onto bare and protein-modified graphite and glassy carbon was demonstrated in the 10-45 degrees C temperature range in the presence of a chromogenic substrate. Modification of the surfa
The Catalytic Activity and Thermal Denaturation of Plasmin Adsorbed to Graphite Carbon Surfaces
β Scribed by Sylvie Longchamp; Hyacinthe N. Randriamahazaka; Jean-Maxime Nigretto
- Publisher
- Elsevier Science
- Year
- 1994
- Tongue
- English
- Weight
- 403 KB
- Volume
- 166
- Category
- Article
- ISSN
- 0021-9797
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β¦ Synopsis
We report the catalytic properties of plasmin irreversibly adsorbed to surfaces made of a mixture of graphite carbon with minel (graphite earlon paste). The assay of the immobilized enzyme was achieved, under forced convection, with a specific and chromogenic substrate (S-2251) dissolved in the solution, under varying temperatures and (\mathrm{pH}) conditions. Results showed that these two variables affected more critically the activity of the adsorbed enzyme than that of the free form. Also differences observed in the respective activity vs (\mathrm{pH}) relationships suggested that the coated surface was able to discriminate between different isoelectric forms of plasmin. Time-varying activities observed in the temperature range (10-30^{\circ} \mathrm{C}) were interpretated in terms of the first-ordered thermal denaturation reaction, which affected some of the adsorbed plasmin forms. 1994 Academic Press. Inc.
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