Characterization of the cysteinyl-containing peptides of the gamma subunit of coupling factor 1
The cysteinyl peptides of the gamma subunit of chloroplast coupling factor 1 (CF1) have been analyzed by high performance liquid chromatography. Analysis of the reduced enzyme alkylated with 4-vinylpyridine showed that the gamma subunit contains four cysteinyl residues. Two of these residues are inv...
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| Veröffentlicht in: | The Journal of biological chemistry 1984-06, Vol.259 (11), p.7281-7285 |
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| container_title | The Journal of biological chemistry |
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| creator | Moroney, J V Fullmer, C S McCarty, R E |
| description | The cysteinyl peptides of the gamma subunit of chloroplast coupling factor 1 (CF1) have been analyzed by high performance liquid chromatography. Analysis of the reduced enzyme alkylated with 4-vinylpyridine showed that the gamma subunit contains four cysteinyl residues. Two of these residues are involved in a disulfide linkage in CF1 either in solution or bound to washed thylakoid membranes. Two free sulfhydryls, one that is readily attacked by alkylating reagents and another that is less reactive, were also detected. Each of these four cysteinyl residues is present in a separate tryptic peptide derived from the gamma subunit. These results show that 4-vinylpyridine is an excellent reagent for the analysis of cysteinyl-containing peptides and support our analyses of the roles of cysteinyl residues in the gamma subunit in ATP synthesis and hydrolysis. |
| doi_str_mv | 10.1016/S0021-9258(17)39869-1 |
| format | Article |
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Analysis of the reduced enzyme alkylated with 4-vinylpyridine showed that the gamma subunit contains four cysteinyl residues. Two of these residues are involved in a disulfide linkage in CF1 either in solution or bound to washed thylakoid membranes. Two free sulfhydryls, one that is readily attacked by alkylating reagents and another that is less reactive, were also detected. Each of these four cysteinyl residues is present in a separate tryptic peptide derived from the gamma subunit. These results show that 4-vinylpyridine is an excellent reagent for the analysis of cysteinyl-containing peptides and support our analyses of the roles of cysteinyl residues in the gamma subunit in ATP synthesis and hydrolysis.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)39869-1</identifier><identifier>PMID: 6233281</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Amino Acids - analysis ; Biological and medical sciences ; Cell structures and functions ; Chloroplast, photosynthetic membrane and photosynthesis ; Chromatography, High Pressure Liquid ; Cysteine - analysis ; Dithiothreitol - pharmacology ; Ethylmaleimide - pharmacology ; Fundamental and applied biological sciences. Psychology ; Macromolecular Substances ; Molecular and cellular biology ; Peptide Fragments - analysis ; Plants - enzymology ; Proton-Translocating ATPases - analysis ; Pyridines - pharmacology ; Trypsin - metabolism</subject><ispartof>The Journal of biological chemistry, 1984-06, Vol.259 (11), p.7281-7285</ispartof><rights>1984 © 1984 ASBMB. 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Analysis of the reduced enzyme alkylated with 4-vinylpyridine showed that the gamma subunit contains four cysteinyl residues. Two of these residues are involved in a disulfide linkage in CF1 either in solution or bound to washed thylakoid membranes. Two free sulfhydryls, one that is readily attacked by alkylating reagents and another that is less reactive, were also detected. Each of these four cysteinyl residues is present in a separate tryptic peptide derived from the gamma subunit. These results show that 4-vinylpyridine is an excellent reagent for the analysis of cysteinyl-containing peptides and support our analyses of the roles of cysteinyl residues in the gamma subunit in ATP synthesis and hydrolysis.</description><subject>Amino Acids - analysis</subject><subject>Biological and medical sciences</subject><subject>Cell structures and functions</subject><subject>Chloroplast, photosynthetic membrane and photosynthesis</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cysteine - analysis</subject><subject>Dithiothreitol - pharmacology</subject><subject>Ethylmaleimide - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Macromolecular Substances</subject><subject>Molecular and cellular biology</subject><subject>Peptide Fragments - analysis</subject><subject>Plants - enzymology</subject><subject>Proton-Translocating ATPases - analysis</subject><subject>Pyridines - pharmacology</subject><subject>Trypsin - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE-r1DAUxYMoz_HpR3hQUEQX1dxk2iQrkcF_8MCFCu5Cmt5OI21Sk1QZP73t6zhbs7mQ-zvnXA4hN0BfAYX69RdKGZSKVfIFiJdcyVqVcI_sgEpe8gq-3ye7C_KQPErpB13eXsEVuaoZ50zCjuhDb6KxGaP7Y7ILvghdkXss7ClldP40lDb4bJx3_lhMOGXXYvoHHc04miLNzexdXj9tmKdhJbvFM8QCHpMHnRkSPjnPa_Lt_buvh4_l7ecPnw5vb0vLhYKyW-4RgiPj-67iTDTKyKpBFIY3ktG6Ab5vVI2VUpJjJxgVTS2wFnUrmOw4vybPN98php8zpqxHlywOg_EY5qQlUCFBiQWsNtDGkFLETk_RjSaeNFC9FqvvitVraxqEvitWw6K7OQfMzYjtRXVuctk_O-9NsmboovHWpQsmFYg9X-Ofbljvjv1vF1E3LtgeR82qJQa02MzebBQulf1yGHWyDr3FdlHYrNvg_nPuX3zSn_8</recordid><startdate>19840610</startdate><enddate>19840610</enddate><creator>Moroney, J V</creator><creator>Fullmer, C S</creator><creator>McCarty, R E</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>19840610</creationdate><title>Characterization of the cysteinyl-containing peptides of the gamma subunit of coupling factor 1</title><author>Moroney, J V ; Fullmer, C S ; McCarty, R E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3791-f233773e234f5327b9a85bee7a3b8206b134b96e59983ef7207b67e676d728f33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Amino Acids - analysis</topic><topic>Biological and medical sciences</topic><topic>Cell structures and functions</topic><topic>Chloroplast, photosynthetic membrane and photosynthesis</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cysteine - analysis</topic><topic>Dithiothreitol - pharmacology</topic><topic>Ethylmaleimide - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Macromolecular Substances</topic><topic>Molecular and cellular biology</topic><topic>Peptide Fragments - analysis</topic><topic>Plants - enzymology</topic><topic>Proton-Translocating ATPases - analysis</topic><topic>Pyridines - pharmacology</topic><topic>Trypsin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moroney, J V</creatorcontrib><creatorcontrib>Fullmer, C S</creatorcontrib><creatorcontrib>McCarty, R E</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moroney, J V</au><au>Fullmer, C S</au><au>McCarty, R E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the cysteinyl-containing peptides of the gamma subunit of coupling factor 1</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1984-06-10</date><risdate>1984</risdate><volume>259</volume><issue>11</issue><spage>7281</spage><epage>7285</epage><pages>7281-7285</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The cysteinyl peptides of the gamma subunit of chloroplast coupling factor 1 (CF1) have been analyzed by high performance liquid chromatography. Analysis of the reduced enzyme alkylated with 4-vinylpyridine showed that the gamma subunit contains four cysteinyl residues. Two of these residues are involved in a disulfide linkage in CF1 either in solution or bound to washed thylakoid membranes. Two free sulfhydryls, one that is readily attacked by alkylating reagents and another that is less reactive, were also detected. Each of these four cysteinyl residues is present in a separate tryptic peptide derived from the gamma subunit. These results show that 4-vinylpyridine is an excellent reagent for the analysis of cysteinyl-containing peptides and support our analyses of the roles of cysteinyl residues in the gamma subunit in ATP synthesis and hydrolysis.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>6233281</pmid><doi>10.1016/S0021-9258(17)39869-1</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1984-06, Vol.259 (11), p.7281-7285 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acids - analysis Biological and medical sciences Cell structures and functions Chloroplast, photosynthetic membrane and photosynthesis Chromatography, High Pressure Liquid Cysteine - analysis Dithiothreitol - pharmacology Ethylmaleimide - pharmacology Fundamental and applied biological sciences. Psychology Macromolecular Substances Molecular and cellular biology Peptide Fragments - analysis Plants - enzymology Proton-Translocating ATPases - analysis Pyridines - pharmacology Trypsin - metabolism |
| title | Characterization of the cysteinyl-containing peptides of the gamma subunit of coupling factor 1 |
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