Use of anion-exchange high-performance liquid chromatography for the study of smooth muscle myosin light-chain kinase and its catalytic domain |
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Authors: | L.Dalla Libera M. Fasolo P. Cavallini E. Ratti G. Gaviraghi |
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Affiliation: | L.Dalla Libera*, M. Fasolo, P. Cavallini, E. Ratti,G. Gaviraghi |
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Abstract: | Avian myosin light-chain kinase from smooth muscle of the gizzard and its catalytic domain, derived from the intact enzyme by trypsin digestion, was purified within 30–40 min by both analytical and preparative anion-exchange high-performance liquid chromatography. The proteins obtained were more than 95% pure and retained their biological activity. The high-performance anion-exchange chromatography protocols represent a significant decrease in purification time when compared with conventional ion-exchange chromatography. |
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