32,000-Dalton Subunit of the 1,4-Dihydropyridine Receptor
Polyclonal antibodies to the 32,000-Da polypeptide of the 1,4-dihydropyridine receptor of the voltage-dependent Ca2+ channel have been produced and used to characterize the association of the 32,000-Da polypeptide (gamma subunit) with other subunits of the dihydropyridine receptor. The 32,000-Da pol...
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| Veröffentlicht in: | Annals of the New York Academy of Sciences 1989-01, Vol.560 (1), p.251-257 |
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| container_title | Annals of the New York Academy of Sciences |
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| creator | CAMPBELL, KEVIN P. SHARP, ALAN H. LEUNG, ALBERT T. |
| description | Polyclonal antibodies to the 32,000-Da polypeptide of the 1,4-dihydropyridine receptor of the voltage-dependent Ca2+ channel have been produced and used to characterize the association of the 32,000-Da polypeptide (gamma subunit) with other subunits of the dihydropyridine receptor. The 32,000-Da polypeptide was found to copurify with alpha 1 and alpha 2 subunits at each step of the purification of the dihydropyridine receptor. Monoclonal antibodies against the alpha 1 and beta subunits immunoprecipitate the digitonin-solubilized dihydropyridine receptor as a multisubunit complex that includes the 32,000-Da polypeptide. Polyclonal antibodies generated against both the nonreduced and reduced forms of the alpha 2 subunit and the gamma subunit have been used to show that the 32,000-Da polypeptide is not a proteolytic fragment of a larger component of the dihydropyridine receptor and not disulfide linked to the alpha 2 subunit. Our results demonstrate that the 32,000-Da polypeptide (gamma subunit) is an integral and distinct component of the dihydropyridine receptor. |
| doi_str_mv | 10.1111/j.1749-6632.1989.tb24102.x |
| format | Article |
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The 32,000-Da polypeptide was found to copurify with alpha 1 and alpha 2 subunits at each step of the purification of the dihydropyridine receptor. Monoclonal antibodies against the alpha 1 and beta subunits immunoprecipitate the digitonin-solubilized dihydropyridine receptor as a multisubunit complex that includes the 32,000-Da polypeptide. Polyclonal antibodies generated against both the nonreduced and reduced forms of the alpha 2 subunit and the gamma subunit have been used to show that the 32,000-Da polypeptide is not a proteolytic fragment of a larger component of the dihydropyridine receptor and not disulfide linked to the alpha 2 subunit. Our results demonstrate that the 32,000-Da polypeptide (gamma subunit) is an integral and distinct component of the dihydropyridine receptor.</description><identifier>ISSN: 0077-8923</identifier><identifier>EISSN: 1749-6632</identifier><identifier>DOI: 10.1111/j.1749-6632.1989.tb24102.x</identifier><identifier>PMID: 2545137</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Calcium Channel Blockers ; Calcium Channels ; Chromatography, Affinity ; Chromatography, Ion Exchange ; Electrophoresis, Polyacrylamide Gel ; Immunoblotting ; Immunosorbent Techniques ; Macromolecular Substances ; Molecular Weight ; Muscles - analysis ; Rabbits ; Receptors, Nicotinic - isolation & purification</subject><ispartof>Annals of the New York Academy of Sciences, 1989-01, Vol.560 (1), p.251-257</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c352t-43e9f2b6bb333967689797635f5e9b6e75872ef4be746da864cc9aa1a7794a293</citedby><cites>FETCH-LOGICAL-c352t-43e9f2b6bb333967689797635f5e9b6e75872ef4be746da864cc9aa1a7794a293</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2545137$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CAMPBELL, KEVIN P.</creatorcontrib><creatorcontrib>SHARP, ALAN H.</creatorcontrib><creatorcontrib>LEUNG, ALBERT T.</creatorcontrib><title>32,000-Dalton Subunit of the 1,4-Dihydropyridine Receptor</title><title>Annals of the New York Academy of Sciences</title><addtitle>Ann N Y Acad Sci</addtitle><description>Polyclonal antibodies to the 32,000-Da polypeptide of the 1,4-dihydropyridine receptor of the voltage-dependent Ca2+ channel have been produced and used to characterize the association of the 32,000-Da polypeptide (gamma subunit) with other subunits of the dihydropyridine receptor. The 32,000-Da polypeptide was found to copurify with alpha 1 and alpha 2 subunits at each step of the purification of the dihydropyridine receptor. Monoclonal antibodies against the alpha 1 and beta subunits immunoprecipitate the digitonin-solubilized dihydropyridine receptor as a multisubunit complex that includes the 32,000-Da polypeptide. Polyclonal antibodies generated against both the nonreduced and reduced forms of the alpha 2 subunit and the gamma subunit have been used to show that the 32,000-Da polypeptide is not a proteolytic fragment of a larger component of the dihydropyridine receptor and not disulfide linked to the alpha 2 subunit. Our results demonstrate that the 32,000-Da polypeptide (gamma subunit) is an integral and distinct component of the dihydropyridine receptor.</description><subject>Animals</subject><subject>Calcium Channel Blockers</subject><subject>Calcium Channels</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, Ion Exchange</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Immunoblotting</subject><subject>Immunosorbent Techniques</subject><subject>Macromolecular Substances</subject><subject>Molecular Weight</subject><subject>Muscles - analysis</subject><subject>Rabbits</subject><subject>Receptors, Nicotinic - isolation & purification</subject><issn>0077-8923</issn><issn>1749-6632</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1Lw0AQhhdRaq3-BCF48NTE_cpO1pu0WpWiUBWPy26ywdQ2ibsJtP_ehIbOZQ7P-87Ag9ANwRHp5m4dEeAyFILRiMhERo2hnGAa7U7Q-IhO0RhjgDCRlJ2jC-_XGBOacBihEY15TBiMkWR0ijEO53rTVGXw0Zq2LJqgyoPmxwZkysN58bPPXFXvXZEVpQ1WNrV1U7lLdJbrjbdXw56gr6fHz9lzuHxfvMwelmHKYtqEnFmZUyOMYYxJASKRIEGwOI-tNMJCnAC1OTcWuMh0IniaSq2JBpBcU8km6PZwt3bVX2t9o7aFT-1mo0tbtV6BxIJzSrrg_SGYusp7Z3NVu2Kr3V4RrHpvaq16OaqXo3pvavCmdl35evjSmq3NjtVBVMfDAy98Y3dHrN2vEsAgVt9vC8VXr0AXJFHA_gFDhna0</recordid><startdate>19890101</startdate><enddate>19890101</enddate><creator>CAMPBELL, KEVIN P.</creator><creator>SHARP, ALAN H.</creator><creator>LEUNG, ALBERT T.</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19890101</creationdate><title>32,000-Dalton Subunit of the 1,4-Dihydropyridine Receptor</title><author>CAMPBELL, KEVIN P. ; SHARP, ALAN H. ; LEUNG, ALBERT T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c352t-43e9f2b6bb333967689797635f5e9b6e75872ef4be746da864cc9aa1a7794a293</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>Calcium Channel Blockers</topic><topic>Calcium Channels</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, Ion Exchange</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Immunoblotting</topic><topic>Immunosorbent Techniques</topic><topic>Macromolecular Substances</topic><topic>Molecular Weight</topic><topic>Muscles - analysis</topic><topic>Rabbits</topic><topic>Receptors, Nicotinic - isolation & purification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CAMPBELL, KEVIN P.</creatorcontrib><creatorcontrib>SHARP, ALAN H.</creatorcontrib><creatorcontrib>LEUNG, ALBERT T.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Annals of the New York Academy of Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CAMPBELL, KEVIN P.</au><au>SHARP, ALAN H.</au><au>LEUNG, ALBERT T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>32,000-Dalton Subunit of the 1,4-Dihydropyridine Receptor</atitle><jtitle>Annals of the New York Academy of Sciences</jtitle><addtitle>Ann N Y Acad Sci</addtitle><date>1989-01-01</date><risdate>1989</risdate><volume>560</volume><issue>1</issue><spage>251</spage><epage>257</epage><pages>251-257</pages><issn>0077-8923</issn><eissn>1749-6632</eissn><abstract>Polyclonal antibodies to the 32,000-Da polypeptide of the 1,4-dihydropyridine receptor of the voltage-dependent Ca2+ channel have been produced and used to characterize the association of the 32,000-Da polypeptide (gamma subunit) with other subunits of the dihydropyridine receptor. The 32,000-Da polypeptide was found to copurify with alpha 1 and alpha 2 subunits at each step of the purification of the dihydropyridine receptor. Monoclonal antibodies against the alpha 1 and beta subunits immunoprecipitate the digitonin-solubilized dihydropyridine receptor as a multisubunit complex that includes the 32,000-Da polypeptide. Polyclonal antibodies generated against both the nonreduced and reduced forms of the alpha 2 subunit and the gamma subunit have been used to show that the 32,000-Da polypeptide is not a proteolytic fragment of a larger component of the dihydropyridine receptor and not disulfide linked to the alpha 2 subunit. Our results demonstrate that the 32,000-Da polypeptide (gamma subunit) is an integral and distinct component of the dihydropyridine receptor.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>2545137</pmid><doi>10.1111/j.1749-6632.1989.tb24102.x</doi><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0077-8923 |
| ispartof | Annals of the New York Academy of Sciences, 1989-01, Vol.560 (1), p.251-257 |
| issn | 0077-8923 1749-6632 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79064421 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Animals Calcium Channel Blockers Calcium Channels Chromatography, Affinity Chromatography, Ion Exchange Electrophoresis, Polyacrylamide Gel Immunoblotting Immunosorbent Techniques Macromolecular Substances Molecular Weight Muscles - analysis Rabbits Receptors, Nicotinic - isolation & purification |
| title | 32,000-Dalton Subunit of the 1,4-Dihydropyridine Receptor |
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