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Biotechnology and Applied Biochemistry (2000) 31, (231–237) (Printed in Great Britain)

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Introduction of thiol-reactive structures on to soluble and insoluble proteins

Carmen Manta*¹, Karen Ovsejevi*, Lorenz Betancor†, Valeria Grazú*, Julio Batistoni‡, Francisco Batista-Viera* and Jan Carlsson§

*Cátedra de Bioquímica, Facultad de Química, CC 1157, Montevideo, Uruguay, †Laboratorio de Bioquímica, Unidad Asociada de la Facultad de Ciencias, Montevideo, Uruguay, ‡Laboratorio de Inmunología, Unidad Asociada de la Facultad de Ciencias, Montevideo, Uruguay, and §Centre for Surface Biotechnology, Biomedical Center, University of Uppsala, P. O. Box 577, S-751 23 Uppsala, Sweden

Abbreviations used: MPP, magnesium monoperoxyphthalate; 2-PDS, 2,2´-dithiopyridine; 2-TP, 2-thiopyridone.

¹ To whom correspondence should be addressed.

When proteins containing disulphide groups were oxidized with magnesium monoperoxyphthalate at acidic pH, they acquired the property of binding thiol compounds. This was the case with the insoluble protein keratin, chosen for having a large number of disulphide bridges, and with soluble ones like BSA and immunoglobulins. The potential applications of some of these modified proteins for the preparation of soluble bioconjugates have been explored. As a particular example of an application, the immobilization of activated IgG on to solid phases might provide a new way for preparing immunoadsorbents.

Received 15 October 1999; accepted 18 October 1999

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