Parvalbumin isoforms in chicken muscle and thymus. Amino acid sequence analysis of muscle parvalbumin by tandem mass spectrometry
Parvalbumins are high-affinity Ca(2+)-binding proteins characterized by an EF-hand structure. Muscles of lower vertebrates contain up to five isoparvalbumins whereas higher vertebrates were believed to contain only one isoform per species. Recently Brewer et al. [Brewer, J.M., Wunderlich, J.K., &...
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| Veröffentlicht in: | Biochemistry (Easton) 1991-09, Vol.30 (36), p.8812-8816 |
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| creator | Kuster, Thomas Staudenmann, Werner Hughes, Graham J Heizmann, Claus W |
| description | Parvalbumins are high-affinity Ca(2+)-binding proteins characterized by an EF-hand structure. Muscles of lower vertebrates contain up to five isoparvalbumins whereas higher vertebrates were believed to contain only one isoform per species. Recently Brewer et al. [Brewer, J.M., Wunderlich, J.K., & Ragland, W. (1990) Biochimie 72, 653-660] purified and sequenced a protein that they named avian thymic hormone, from chicken thymus. This protein, promoting immunological maturation of bone marrow cells in culture, was identified as a parvalbumin. The amino acid composition of this thymic parvalbumin was, however, considerably different from those of chicken muscle parvalbumin [Strehler, E.E., Eppenberger, H.M., & Heizman, C.W. (1977) FEBS Lett. 75, 127-133], suggesting the existence of two tissue-specific parvalbumins in chicken. We purified parvalbumin from chicken muscle, determined its complete amino acid sequence by tandem mass spectrometry, and showed that this protein is rather homologous to muscle parvalbumins from other species but different in 45 positions from the thymic parvalbumin. We discuss the possibility that a parvalbumin gene family might exist in higher vertebrates, expressed in a tissue-specific and developmentally regulated manner. |
| doi_str_mv | 10.1021/bi00100a012 |
| format | Article |
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The amino acid composition of this thymic parvalbumin was, however, considerably different from those of chicken muscle parvalbumin [Strehler, E.E., Eppenberger, H.M., & Heizman, C.W. (1977) FEBS Lett. 75, 127-133], suggesting the existence of two tissue-specific parvalbumins in chicken. We purified parvalbumin from chicken muscle, determined its complete amino acid sequence by tandem mass spectrometry, and showed that this protein is rather homologous to muscle parvalbumins from other species but different in 45 positions from the thymic parvalbumin. We discuss the possibility that a parvalbumin gene family might exist in higher vertebrates, expressed in a tissue-specific and developmentally regulated manner.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00100a012</identifier><identifier>PMID: 1888741</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Amino Acids - isolation & purification ; Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Biological and medical sciences ; Chickens ; Fundamental and applied biological sciences. Psychology ; Humans ; Mass Spectrometry ; Mice ; Molecular Sequence Data ; Muscles - chemistry ; Parvalbumins - chemistry ; Parvalbumins - isolation & purification ; Proteins ; Rabbits ; Rats ; Sequence Alignment ; Sequence Homology, Nucleic Acid ; Stereoisomerism ; Thymus Gland - chemistry</subject><ispartof>Biochemistry (Easton), 1991-09, Vol.30 (36), p.8812-8816</ispartof><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a509t-e6d682b707d0a69142e3f1640a5d8ac0a26b9da514f41fa61f0362c658cc66863</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00100a012$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00100a012$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5181208$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1888741$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kuster, Thomas</creatorcontrib><creatorcontrib>Staudenmann, Werner</creatorcontrib><creatorcontrib>Hughes, Graham J</creatorcontrib><creatorcontrib>Heizmann, Claus W</creatorcontrib><title>Parvalbumin isoforms in chicken muscle and thymus. Amino acid sequence analysis of muscle parvalbumin by tandem mass spectrometry</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Parvalbumins are high-affinity Ca(2+)-binding proteins characterized by an EF-hand structure. Muscles of lower vertebrates contain up to five isoparvalbumins whereas higher vertebrates were believed to contain only one isoform per species. Recently Brewer et al. [Brewer, J.M., Wunderlich, J.K., & Ragland, W. (1990) Biochimie 72, 653-660] purified and sequenced a protein that they named avian thymic hormone, from chicken thymus. This protein, promoting immunological maturation of bone marrow cells in culture, was identified as a parvalbumin. The amino acid composition of this thymic parvalbumin was, however, considerably different from those of chicken muscle parvalbumin [Strehler, E.E., Eppenberger, H.M., & Heizman, C.W. (1977) FEBS Lett. 75, 127-133], suggesting the existence of two tissue-specific parvalbumins in chicken. We purified parvalbumin from chicken muscle, determined its complete amino acid sequence by tandem mass spectrometry, and showed that this protein is rather homologous to muscle parvalbumins from other species but different in 45 positions from the thymic parvalbumin. We discuss the possibility that a parvalbumin gene family might exist in higher vertebrates, expressed in a tissue-specific and developmentally regulated manner.</description><subject>Amino Acid Sequence</subject><subject>Amino Acids - isolation & purification</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Binding and carrier proteins</subject><subject>Biological and medical sciences</subject><subject>Chickens</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Mass Spectrometry</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Muscles - chemistry</subject><subject>Parvalbumins - chemistry</subject><subject>Parvalbumins - isolation & purification</subject><subject>Proteins</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Stereoisomerism</subject><subject>Thymus Gland - chemistry</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS1EVZbCiTOSDwgOVcrYGzvOsRRoEZWooHC1Jo6jus3H4kkQOfKf422W0gMSp5nR-83Tkx5jzwQcCZDidRUABACCkA_YSigJWV6W6iFbAYDOZKnhEXtMdJ3OHIp8n-0LY0yRixX7dYHxB7bV1IWeBxqaIXbE0-6ugrvxPe8mcq3n2Nd8vJrTdcSPEztwdKHm5L9PvndbHduZAvGh-fOyuedczXxMFr7jHRJx2ng3xqHzY5yfsL0GW_JPd_OAfX3_7vLkLDv_dPrh5Pg8QwXlmHldayOrAooaUJcil37dCJ0DqtqgA5S6KmtUIm9y0aAWDay1dFoZ57Q2en3AXi6-mzik0DTaLpDzbYu9HyayhQRTCDD_BYUGowq9BQ8X0MWBKPrGbmLoMM5WgN02Y-81k-jnO9up6nz9l12qSPqLnY7ksG0i9i7QHaaEEfI2XbZggUb_807GeGN1sS6Uvbz4Yj9-A3P29o2ynxP_auHRkb0eppiKon8G_A3wn7Jc</recordid><startdate>19910901</startdate><enddate>19910901</enddate><creator>Kuster, Thomas</creator><creator>Staudenmann, Werner</creator><creator>Hughes, Graham J</creator><creator>Heizmann, Claus W</creator><general>American Chemical Society</general><scope>BSCLL</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19910901</creationdate><title>Parvalbumin isoforms in chicken muscle and thymus. Amino acid sequence analysis of muscle parvalbumin by tandem mass spectrometry</title><author>Kuster, Thomas ; Staudenmann, Werner ; Hughes, Graham J ; Heizmann, Claus W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a509t-e6d682b707d0a69142e3f1640a5d8ac0a26b9da514f41fa61f0362c658cc66863</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acids - isolation & purification</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Binding and carrier proteins</topic><topic>Biological and medical sciences</topic><topic>Chickens</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Mass Spectrometry</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Muscles - chemistry</topic><topic>Parvalbumins - chemistry</topic><topic>Parvalbumins - isolation & purification</topic><topic>Proteins</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Stereoisomerism</topic><topic>Thymus Gland - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kuster, Thomas</creatorcontrib><creatorcontrib>Staudenmann, Werner</creatorcontrib><creatorcontrib>Hughes, Graham J</creatorcontrib><creatorcontrib>Heizmann, Claus W</creatorcontrib><collection>Istex</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kuster, Thomas</au><au>Staudenmann, Werner</au><au>Hughes, Graham J</au><au>Heizmann, Claus W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Parvalbumin isoforms in chicken muscle and thymus. Amino acid sequence analysis of muscle parvalbumin by tandem mass spectrometry</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1991-09-01</date><risdate>1991</risdate><volume>30</volume><issue>36</issue><spage>8812</spage><epage>8816</epage><pages>8812-8816</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Parvalbumins are high-affinity Ca(2+)-binding proteins characterized by an EF-hand structure. Muscles of lower vertebrates contain up to five isoparvalbumins whereas higher vertebrates were believed to contain only one isoform per species. Recently Brewer et al. [Brewer, J.M., Wunderlich, J.K., & Ragland, W. (1990) Biochimie 72, 653-660] purified and sequenced a protein that they named avian thymic hormone, from chicken thymus. This protein, promoting immunological maturation of bone marrow cells in culture, was identified as a parvalbumin. The amino acid composition of this thymic parvalbumin was, however, considerably different from those of chicken muscle parvalbumin [Strehler, E.E., Eppenberger, H.M., & Heizman, C.W. (1977) FEBS Lett. 75, 127-133], suggesting the existence of two tissue-specific parvalbumins in chicken. We purified parvalbumin from chicken muscle, determined its complete amino acid sequence by tandem mass spectrometry, and showed that this protein is rather homologous to muscle parvalbumins from other species but different in 45 positions from the thymic parvalbumin. We discuss the possibility that a parvalbumin gene family might exist in higher vertebrates, expressed in a tissue-specific and developmentally regulated manner.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>1888741</pmid><doi>10.1021/bi00100a012</doi><tpages>5</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1991-09, Vol.30 (36), p.8812-8816 |
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| subjects | Amino Acid Sequence Amino Acids - isolation & purification Analytical, structural and metabolic biochemistry Animals Binding and carrier proteins Biological and medical sciences Chickens Fundamental and applied biological sciences. Psychology Humans Mass Spectrometry Mice Molecular Sequence Data Muscles - chemistry Parvalbumins - chemistry Parvalbumins - isolation & purification Proteins Rabbits Rats Sequence Alignment Sequence Homology, Nucleic Acid Stereoisomerism Thymus Gland - chemistry |
| title | Parvalbumin isoforms in chicken muscle and thymus. Amino acid sequence analysis of muscle parvalbumin by tandem mass spectrometry |
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