A High-Affinity Hemoglobin Is Expressed in the Notochord of Amphioxus, Branchiostoma californiense
In the phylum Chordata, only members of the subphylum Vertebrata were thought to express hemoglobin (Hb). Here we document the existence of intracellular Hb expressed in members of the subphylum Cephalochordata. Hemoglobin is expressed in myotome tissue and in notochord cells within the body of amph...
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| Veröffentlicht in: | The Biological bulletin 1998-12, Vol.195 (3), p.255-259 |
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| container_title | The Biological bulletin |
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| creator | Bishop, Jamie J. Vandergon, Thomas L. Green, David B. Doeller, Jeannette E. Kraus, David W. |
| description | In the phylum Chordata, only members of the subphylum Vertebrata were thought to express hemoglobin (Hb). Here we document the existence of intracellular Hb expressed in members of the subphylum Cephalochordata. Hemoglobin is expressed in myotome tissue and in notochord cells within the body of amphioxus. Both notochord and myotome tissue Hbs have a molecular size consistent with a dimeric molecule made up of two non-covalently linked monomers each of approximately 19 kD. The notochord Hb has a relatively high oxygen-binding affinity, with an apparent P5O of 0.036 kPa (0.27mm Hg), and it does not bind oxygen cooperatively. The notochord Hb may be involved in facilitating oxygen delivery and providing a short-term oxygen store within the notochord cells in order to maintain a high level of aerobic metabolism in support of the sustained contraction necessary for notochord function. |
| doi_str_mv | 10.2307/1543136 |
| format | Article |
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Here we document the existence of intracellular Hb expressed in members of the subphylum Cephalochordata. Hemoglobin is expressed in myotome tissue and in notochord cells within the body of amphioxus. Both notochord and myotome tissue Hbs have a molecular size consistent with a dimeric molecule made up of two non-covalently linked monomers each of approximately 19 kD. The notochord Hb has a relatively high oxygen-binding affinity, with an apparent P5O of 0.036 kPa (0.27mm Hg), and it does not bind oxygen cooperatively. The notochord Hb may be involved in facilitating oxygen delivery and providing a short-term oxygen store within the notochord cells in order to maintain a high level of aerobic metabolism in support of the sustained contraction necessary for notochord function.</description><identifier>ISSN: 0006-3185</identifier><identifier>EISSN: 1939-8697</identifier><identifier>DOI: 10.2307/1543136</identifier><identifier>PMID: 28297607</identifier><language>eng</language><publisher>United States: Marine Biological Laboratory</publisher><subject>Absorption spectra ; Animals ; Branchiostoma californiense ; Cephalochordata ; Chordata ; Chordates ; Chromatography ; Embryonic structures ; Hemoglobin ; Hemoglobins ; Marine ; Molecular evolution ; Oxygen ; Research Notes ; Sodium ; Vertebrates ; Visible spectrum</subject><ispartof>The Biological bulletin, 1998-12, Vol.195 (3), p.255-259</ispartof><rights>Copyright 1998 The Marine Biological Laboratory</rights><rights>Copyright © 1998 by Marine Biological Laboratory</rights><rights>COPYRIGHT 1998 University of Chicago Press</rights><rights>COPYRIGHT 1998 University of Chicago Press</rights><rights>In copyright. Digitized with the permission of the rights holder. http://creativecommons.org/licenses/by-nc-sa/3.0</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c680t-d7c926891652664b8fce6da07d367f64fe29d1e12416c00dbe4fff2b31f5a42b3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/1543136$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/1543136$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28297607$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bishop, Jamie J.</creatorcontrib><creatorcontrib>Vandergon, Thomas L.</creatorcontrib><creatorcontrib>Green, David B.</creatorcontrib><creatorcontrib>Doeller, Jeannette E.</creatorcontrib><creatorcontrib>Kraus, David W.</creatorcontrib><title>A High-Affinity Hemoglobin Is Expressed in the Notochord of Amphioxus, Branchiostoma californiense</title><title>The Biological bulletin</title><addtitle>Biol Bull</addtitle><description>In the phylum Chordata, only members of the subphylum Vertebrata were thought to express hemoglobin (Hb). Here we document the existence of intracellular Hb expressed in members of the subphylum Cephalochordata. Hemoglobin is expressed in myotome tissue and in notochord cells within the body of amphioxus. Both notochord and myotome tissue Hbs have a molecular size consistent with a dimeric molecule made up of two non-covalently linked monomers each of approximately 19 kD. The notochord Hb has a relatively high oxygen-binding affinity, with an apparent P5O of 0.036 kPa (0.27mm Hg), and it does not bind oxygen cooperatively. The notochord Hb may be involved in facilitating oxygen delivery and providing a short-term oxygen store within the notochord cells in order to maintain a high level of aerobic metabolism in support of the sustained contraction necessary for notochord function.</description><subject>Absorption spectra</subject><subject>Animals</subject><subject>Branchiostoma californiense</subject><subject>Cephalochordata</subject><subject>Chordata</subject><subject>Chordates</subject><subject>Chromatography</subject><subject>Embryonic structures</subject><subject>Hemoglobin</subject><subject>Hemoglobins</subject><subject>Marine</subject><subject>Molecular evolution</subject><subject>Oxygen</subject><subject>Research Notes</subject><subject>Sodium</subject><subject>Vertebrates</subject><subject>Visible spectrum</subject><issn>0006-3185</issn><issn>1939-8697</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>79B</sourceid><recordid>eNqN0l1r2zAUBmAzNtasG_sHwxf76CDeJNmW5cssdE0gtBfbroUsHzkKtuRKdkn__dQ5HQSyUXQhzuHhoI83it5i9IWkqPiK8yzFKX0WzXCZlgmjZfE8miGEaJJilp9Fr7zfhRIRnL2MzggjZUFRMYuqRbzSzTZZKKWNHu7jFXS2aW2lTbz28eW-d-A91HGohy3E13awcmtdHVsVL7p-q-1-9PP4mxNGhsIPthOxFK1W1hkNxsPr6IUSrYc3h_08-vX98udylWxurtbLxSaRlKEhqQtZEspKTHNCaVYxJYHWAhV1SgtFMwWkrDFgkmEqEaoryJRSpEqxykUW9vNoPc31nR623hotDK-0rfUdOB_uxu8It0If9VpdOeHuuXUN74UbOMlpisKsi2lW7-ztCH7gnfYS2lYYsKPnmBUMFyVDZaAf_08LkpcI5QHOJ9iIFrg2yg5OyAYMONFaA0qH9iJPyywnOQs8OcHDqqHT8pS_OPKBDLAfGjF6z9c_rp9K2dXmiM5PUWnbFhrg4QOXN0f808Sls947ULx3unt4YIz4Q1L5IalBvjs821h1UP91j9EM4PMExpArKRr7J4l8Z0dnQoweB_G-VsF-eIoN7v3kdiGn7p9n-w1IXwkW</recordid><startdate>19981201</startdate><enddate>19981201</enddate><creator>Bishop, Jamie J.</creator><creator>Vandergon, Thomas L.</creator><creator>Green, David B.</creator><creator>Doeller, Jeannette E.</creator><creator>Kraus, David W.</creator><general>Marine Biological Laboratory</general><general>University of Chicago Press</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8GL</scope><scope>ISN</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope><scope>79B</scope></search><sort><creationdate>19981201</creationdate><title>A High-Affinity Hemoglobin Is Expressed in the Notochord of Amphioxus, Branchiostoma californiense</title><author>Bishop, Jamie J. ; Vandergon, Thomas L. ; Green, David B. ; Doeller, Jeannette E. ; Kraus, David W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c680t-d7c926891652664b8fce6da07d367f64fe29d1e12416c00dbe4fff2b31f5a42b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Absorption spectra</topic><topic>Animals</topic><topic>Branchiostoma californiense</topic><topic>Cephalochordata</topic><topic>Chordata</topic><topic>Chordates</topic><topic>Chromatography</topic><topic>Embryonic structures</topic><topic>Hemoglobin</topic><topic>Hemoglobins</topic><topic>Marine</topic><topic>Molecular evolution</topic><topic>Oxygen</topic><topic>Research Notes</topic><topic>Sodium</topic><topic>Vertebrates</topic><topic>Visible spectrum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bishop, Jamie J.</creatorcontrib><creatorcontrib>Vandergon, Thomas L.</creatorcontrib><creatorcontrib>Green, David B.</creatorcontrib><creatorcontrib>Doeller, Jeannette E.</creatorcontrib><creatorcontrib>Kraus, David W.</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: High School</collection><collection>Gale In Context: Canada</collection><collection>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><collection>Biodiversity Heritage Library</collection><jtitle>The Biological bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bishop, Jamie J.</au><au>Vandergon, Thomas L.</au><au>Green, David B.</au><au>Doeller, Jeannette E.</au><au>Kraus, David W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A High-Affinity Hemoglobin Is Expressed in the Notochord of Amphioxus, Branchiostoma californiense</atitle><jtitle>The Biological bulletin</jtitle><addtitle>Biol Bull</addtitle><date>1998-12-01</date><risdate>1998</risdate><volume>195</volume><issue>3</issue><spage>255</spage><epage>259</epage><pages>255-259</pages><issn>0006-3185</issn><eissn>1939-8697</eissn><abstract>In the phylum Chordata, only members of the subphylum Vertebrata were thought to express hemoglobin (Hb). 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| ispartof | The Biological bulletin, 1998-12, Vol.195 (3), p.255-259 |
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| source | Jstor Complete Legacy; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Absorption spectra Animals Branchiostoma californiense Cephalochordata Chordata Chordates Chromatography Embryonic structures Hemoglobin Hemoglobins Marine Molecular evolution Oxygen Research Notes Sodium Vertebrates Visible spectrum |
| title | A High-Affinity Hemoglobin Is Expressed in the Notochord of Amphioxus, Branchiostoma californiense |
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