Sodium-specific channels can be functionally identified in phosphatidylcholine liposomes incorporating detergent-solubilized membrane proteins from pig lens epithelium and outer cortex. The transport of sodium is saturable, specific and protease-sensitive. MIP26 was identified in the solubilized membrane fraction and in the liposomes by means of Western blot analysis. Pre-treatment of liposomes with anti-MIP26 antiserum abolished the transport of sodium. These data indicate that MIP26 is associated to a sodium selective transport activity.

Lens sodium channels are inactivated by anti-MIP26 antibodies / G., Alberti; Gandolfi, Stefano; G., Maraini. - In: EXPERIMENTAL EYE RESEARCH. - ISSN 0014-4835. - 57:(1993), pp. 653-658.

Lens sodium channels are inactivated by anti-MIP26 antibodies

GANDOLFI, Stefano;
1993-01-01

Abstract

Sodium-specific channels can be functionally identified in phosphatidylcholine liposomes incorporating detergent-solubilized membrane proteins from pig lens epithelium and outer cortex. The transport of sodium is saturable, specific and protease-sensitive. MIP26 was identified in the solubilized membrane fraction and in the liposomes by means of Western blot analysis. Pre-treatment of liposomes with anti-MIP26 antiserum abolished the transport of sodium. These data indicate that MIP26 is associated to a sodium selective transport activity.
1993
Lens sodium channels are inactivated by anti-MIP26 antibodies / G., Alberti; Gandolfi, Stefano; G., Maraini. - In: EXPERIMENTAL EYE RESEARCH. - ISSN 0014-4835. - 57:(1993), pp. 653-658.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11381/2437284
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