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Purification of functionally intact 1,4-dihydropyridine receptor from rabbit skeletal muscle by HPLC

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Summary

Functionally intact 1,4-dihydropyridine receptors have been isolated from digitonin-solubilized skeletal muscle membranes with the combined use of Wheatgerm Lectin-Sepharose affinity chromatography and ion-exchange HPLC. Lectin affinity chromatography was used for the purification of glycoproteins containing N-acetyl-glucosamines residues. Separation of functionally intact 1,4-dihydropyridine receptor/calcium channel complex from Mg2+-ATPase, one of the most abundant glycoproteins in skeletal muscle T-tubular membranes, was successfully performed by HPLC on a TSKgel DEAE-5PW column.

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Authors and Affiliations

  1. Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, 45267-0575, Cincinnati, OH, USA

    H. Kalász & P. L. Vaghy

  2. Department of Chemical Engineering, Yale University, P.O. Box 2159, 06520, New Haven, CT, USA

    Cs. Horváth

Authors
  1. H. Kalász
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  2. Cs. Horváth
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  3. P. L. Vaghy
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Kalász, H., Horváth, C. & Vaghy, P.L. Purification of functionally intact 1,4-dihydropyridine receptor from rabbit skeletal muscle by HPLC. Chromatographia 30, 533–536 (1990). https://doi.org/10.1007/BF02269800

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  • DOI: https://doi.org/10.1007/BF02269800

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