Aspartate aminotransferase immobilized on collagen films. Activity of dissociated subunits. |
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| Authors: | M Arrio-Dupont P R Coulet |
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| Affiliation: | 1. Laboratoire d''Enzymologie physicochimique et moléculaire, G.R. 13 du CNRS, Université de Paris-Sud, centre d''Orsay, Bat. 433, 91405 Orsay, France;2. Laboratoire de Biologie et Technologie des Membranes du CNRS, Université Claude Bernard de Lyon I, 43, boulevard du 11 novembre 1918, 69621 Villeurbanne, France |
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| Abstract: | Aspartate aminotransferase has been covalently bound to insoluble films of collagen. The immobilized subunits of holoenzyme obtained after alkaline dissociation were inactive but their activity was recovered by incubation with either active enzyme, reduced holoenzyme, or apoenzyme. It was also possible to reduce the bound subunits by sodium borohydride and to reassociate them with native subunits of holoenzyme. |
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