Purification and characterization of the dihydropyridine-sensitive voltage-dependent calcium channel from cardiac tissue. Cooper, C. L., Vandaele, S., Barhanin, J., Fosset, M., Lazdunski, M., & Hosey, M. M The Journal of Biological Chemistry, 262(2):509--512, 1987. abstract bibtex The dihydropyridine-sensitive voltage-dependent Ca2+ channel from cardiac tissue was purified 900-fold using DEAE-Sephadex A-25, concanavalin A-Sepharose, and wheat germ agglutinin-Sepharose. The purified preparation was highly enriched in a peptide of 140,000 daltons when electrophoresed on sodium dodecyl sulfate gels in the presence of 2-mercaptoethanol, or 170,000 when electrophoresed in the presence of iodoacetamide. Polyclonal antibodies raised against the purified subunits of the rabbit skeletal muscle Ca2+ channel recognized the 170-kDa protein in preparations electrophoresed under nonreducing conditions, and the large peptide of 140 kDa and smaller peptides of 29-32 kDa in preparations analyzed under reducing conditions. Monoclonal antibodies, which were raised against the native Ca2+ channel from skeletal muscle, immunoprecipitated [3H]PN 200-110 binding activity from solubilized cardiac membranes and immunoprecipitated 125I-labeled peptides (from the purified cardiac Ca2+ channel preparation) which migrated as a single species of 170 kDa under nonreducing conditions, or as 140, 32, and 29 kDa under reducing conditions. The results show that the purified cardiac Ca2+ channel, like that previously purified from skeletal muscle, consists of a major component of 170 kDa which is comprised of a 140-kDa peptide linked by disulfide bonds to smaller peptides of 32-29 kDa. Peptide maps of the 140-kDa peptide purified from cardiac and skeletal muscle preparations were strikingly similar, suggesting a high degree of homology in their primary sequence
@article{cooper_purification_1987,
title = {Purification and characterization of the dihydropyridine-sensitive voltage-dependent calcium channel from cardiac tissue},
volume = {262},
issn = {00219258},
abstract = {The dihydropyridine-sensitive voltage-dependent Ca2+ channel from cardiac tissue was purified 900-fold using DEAE-Sephadex A-25, concanavalin A-Sepharose, and wheat germ agglutinin-Sepharose. The purified preparation was highly enriched in a peptide of 140,000 daltons when electrophoresed on sodium dodecyl sulfate gels in the presence of 2-mercaptoethanol, or 170,000 when electrophoresed in the presence of iodoacetamide. Polyclonal antibodies raised against the purified subunits of the rabbit skeletal muscle Ca2+ channel recognized the 170-kDa protein in preparations electrophoresed under nonreducing conditions, and the large peptide of 140 kDa and smaller peptides of 29-32 kDa in preparations analyzed under reducing conditions. Monoclonal antibodies, which were raised against the native Ca2+ channel from skeletal muscle, immunoprecipitated [3H]PN 200-110 binding activity from solubilized cardiac membranes and immunoprecipitated 125I-labeled peptides (from the purified cardiac Ca2+ channel preparation) which migrated as a single species of 170 kDa under nonreducing conditions, or as 140, 32, and 29 kDa under reducing conditions. The results show that the purified cardiac Ca2+ channel, like that previously purified from skeletal muscle, consists of a major component of 170 kDa which is comprised of a 140-kDa peptide linked by disulfide bonds to smaller peptides of 32-29 kDa. Peptide maps of the 140-kDa peptide purified from cardiac and skeletal muscle preparations were strikingly similar, suggesting a high degree of homology in their primary sequence},
number = {2},
journal = {The Journal of Biological Chemistry},
author = {Cooper, Christy L. and Vandaele, Sylvie and Barhanin, Jacques and Fosset, Michel and Lazdunski, Michel and Hosey, Marlene M},
year = {1987},
pmid = {2433268},
keywords = {Recherche biomédicale},
pages = {509--512}
}
Downloads: 0
{"_id":"REmago4DNXuP7Dygr","bibbaseid":"cooper-vandaele-barhanin-fosset-lazdunski-hosey-purificationandcharacterizationofthedihydropyridinesensitivevoltagedependentcalciumchannelfromcardiactissue-1987","downloads":0,"creationDate":"2017-02-08T17:46:11.574Z","title":"Purification and characterization of the dihydropyridine-sensitive voltage-dependent calcium channel from cardiac tissue","author_short":["Cooper, C. L.","Vandaele, S.","Barhanin, J.","Fosset, M.","Lazdunski, M.","Hosey, M. M"],"year":1987,"bibtype":"article","biburl":"http://bibbase.org/zotero/Biomettico","bibdata":{"bibtype":"article","type":"article","title":"Purification and characterization of the dihydropyridine-sensitive voltage-dependent calcium channel from cardiac tissue","volume":"262","issn":"00219258","abstract":"The dihydropyridine-sensitive voltage-dependent Ca2+ channel from cardiac tissue was purified 900-fold using DEAE-Sephadex A-25, concanavalin A-Sepharose, and wheat germ agglutinin-Sepharose. The purified preparation was highly enriched in a peptide of 140,000 daltons when electrophoresed on sodium dodecyl sulfate gels in the presence of 2-mercaptoethanol, or 170,000 when electrophoresed in the presence of iodoacetamide. Polyclonal antibodies raised against the purified subunits of the rabbit skeletal muscle Ca2+ channel recognized the 170-kDa protein in preparations electrophoresed under nonreducing conditions, and the large peptide of 140 kDa and smaller peptides of 29-32 kDa in preparations analyzed under reducing conditions. Monoclonal antibodies, which were raised against the native Ca2+ channel from skeletal muscle, immunoprecipitated [3H]PN 200-110 binding activity from solubilized cardiac membranes and immunoprecipitated 125I-labeled peptides (from the purified cardiac Ca2+ channel preparation) which migrated as a single species of 170 kDa under nonreducing conditions, or as 140, 32, and 29 kDa under reducing conditions. The results show that the purified cardiac Ca2+ channel, like that previously purified from skeletal muscle, consists of a major component of 170 kDa which is comprised of a 140-kDa peptide linked by disulfide bonds to smaller peptides of 32-29 kDa. Peptide maps of the 140-kDa peptide purified from cardiac and skeletal muscle preparations were strikingly similar, suggesting a high degree of homology in their primary sequence","number":"2","journal":"The Journal of Biological Chemistry","author":[{"propositions":[],"lastnames":["Cooper"],"firstnames":["Christy","L."],"suffixes":[]},{"propositions":[],"lastnames":["Vandaele"],"firstnames":["Sylvie"],"suffixes":[]},{"propositions":[],"lastnames":["Barhanin"],"firstnames":["Jacques"],"suffixes":[]},{"propositions":[],"lastnames":["Fosset"],"firstnames":["Michel"],"suffixes":[]},{"propositions":[],"lastnames":["Lazdunski"],"firstnames":["Michel"],"suffixes":[]},{"propositions":[],"lastnames":["Hosey"],"firstnames":["Marlene","M"],"suffixes":[]}],"year":"1987","pmid":"2433268","keywords":"Recherche biomédicale","pages":"509--512","bibtex":"@article{cooper_purification_1987,\n\ttitle = {Purification and characterization of the dihydropyridine-sensitive voltage-dependent calcium channel from cardiac tissue},\n\tvolume = {262},\n\tissn = {00219258},\n\tabstract = {The dihydropyridine-sensitive voltage-dependent Ca2+ channel from cardiac tissue was purified 900-fold using DEAE-Sephadex A-25, concanavalin A-Sepharose, and wheat germ agglutinin-Sepharose. The purified preparation was highly enriched in a peptide of 140,000 daltons when electrophoresed on sodium dodecyl sulfate gels in the presence of 2-mercaptoethanol, or 170,000 when electrophoresed in the presence of iodoacetamide. Polyclonal antibodies raised against the purified subunits of the rabbit skeletal muscle Ca2+ channel recognized the 170-kDa protein in preparations electrophoresed under nonreducing conditions, and the large peptide of 140 kDa and smaller peptides of 29-32 kDa in preparations analyzed under reducing conditions. Monoclonal antibodies, which were raised against the native Ca2+ channel from skeletal muscle, immunoprecipitated [3H]PN 200-110 binding activity from solubilized cardiac membranes and immunoprecipitated 125I-labeled peptides (from the purified cardiac Ca2+ channel preparation) which migrated as a single species of 170 kDa under nonreducing conditions, or as 140, 32, and 29 kDa under reducing conditions. The results show that the purified cardiac Ca2+ channel, like that previously purified from skeletal muscle, consists of a major component of 170 kDa which is comprised of a 140-kDa peptide linked by disulfide bonds to smaller peptides of 32-29 kDa. Peptide maps of the 140-kDa peptide purified from cardiac and skeletal muscle preparations were strikingly similar, suggesting a high degree of homology in their primary sequence},\n\tnumber = {2},\n\tjournal = {The Journal of Biological Chemistry},\n\tauthor = {Cooper, Christy L. and Vandaele, Sylvie and Barhanin, Jacques and Fosset, Michel and Lazdunski, Michel and Hosey, Marlene M},\n\tyear = {1987},\n\tpmid = {2433268},\n\tkeywords = {Recherche biomédicale},\n\tpages = {509--512}\n}\n\n","author_short":["Cooper, C. L.","Vandaele, S.","Barhanin, J.","Fosset, M.","Lazdunski, M.","Hosey, M. M"],"key":"cooper_purification_1987","id":"cooper_purification_1987","bibbaseid":"cooper-vandaele-barhanin-fosset-lazdunski-hosey-purificationandcharacterizationofthedihydropyridinesensitivevoltagedependentcalciumchannelfromcardiactissue-1987","role":"author","urls":{},"keyword":["Recherche biomédicale"],"downloads":0},"search_terms":["purification","characterization","dihydropyridine","sensitive","voltage","dependent","calcium","channel","cardiac","tissue","cooper","vandaele","barhanin","fosset","lazdunski","hosey"],"keywords":["recherche","scientifique","recherche biomédicale"],"authorIDs":[],"dataSources":["ZtKbrGevxC74Q7RNa"]}