Abstract
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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