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  • Title: Detection of the associated state of membrane proteins by polyacrylamide gradient gel electrophoresis with non-denaturing detergents. Application to band 3 protein from erythrocyte membranes.
    Author: Nakashima H, Nakagawa Y, Makino S.
    Journal: Biochim Biophys Acta; 1981 May 20; 643(3):509-18. PubMed ID: 7248287.
    Abstract:
    Polyacrylamide gradient gel electrophoresis was carried out in micellar solutions of various detergents which differ in degree of potency to denature proteins. From the application of this method to band 3 protein from erythrocyte membranes, it was suggested that the procedure was useful in studying the molecular state of membrane proteins. The electrophoretic behaviors of human and bovine band 3 protein did not show any species specificity in either a denature state and a state resembling the native state. As well as in nonionic detergent solutions, the dimeric and tetrameric structures of bovine band 3 protein were preserved in sodium deoxycholate solution, in which protein complexes maintained in nonionic detergent solutions are frequently dissociated. Even in dodecyltrimethylammonium bromide solution, which is a denaturant for water-soluble proteins, part of the band 3 protein was still present as the oligomer. The results suggest that the oligomeric form of band 3 protein is the stable structure and that the dimer and tetramer possibly coexist in membranes.
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