Purification and Functional Properties of the Hemoglobin Components from the Rat (Wistar)
Homogeneous components of Wistar rat hemoglobin have been isolated and characterized from the molecular and functional point of view. The O2 equilibrium behaviour of the three main components (HbII, HbIII, HbIVA) has been investigated as a function of pH and organic phosphate concentration. The liga...
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Veröffentlicht in: | European journal of biochemistry 1981-05, Vol.116 (2), p.243-247 |
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container_title | European journal of biochemistry |
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creator | CONDÒ, Saverio G. GIARDINA, Bruno BARRA, Donatella GILL, Stanley J. BRUNORI, Maurizio |
description | Homogeneous components of Wistar rat hemoglobin have been isolated and characterized from the molecular and functional point of view. The O2 equilibrium behaviour of the three main components (HbII, HbIII, HbIVA) has been investigated as a function of pH and organic phosphate concentration.
The ligand‐binding kinetics of the isolated components have been also studied and are fully consistent with their equilibrium behaviour. It should be remarked that the choice of the system was governed largely by the ability of rat hemoglobins to crystallize very quickly. This almost unique molecular property together with the complete reversibility of the process may allow information to be obtained on the thermodynamics of ligand linked phase changes. |
doi_str_mv | 10.1111/j.1432-1033.1981.tb05325.x |
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The ligand‐binding kinetics of the isolated components have been also studied and are fully consistent with their equilibrium behaviour. It should be remarked that the choice of the system was governed largely by the ability of rat hemoglobins to crystallize very quickly. This almost unique molecular property together with the complete reversibility of the process may allow information to be obtained on the thermodynamics of ligand linked phase changes.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1981.tb05325.x</identifier><identifier>PMID: 7250126</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Hemoglobins - isolation & purification ; Hydrogen-Ion Concentration ; Isoelectric Focusing ; Kinetics ; Oxyhemoglobins - metabolism ; Photolysis ; Phytic Acid - pharmacology ; Rats ; Solubility</subject><ispartof>European journal of biochemistry, 1981-05, Vol.116 (2), p.243-247</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4223-81b669110bd41c5eb1402d6fa2ed2124969546d2aa58ad568e33e4cccba723873</citedby><cites>FETCH-LOGICAL-c4223-81b669110bd41c5eb1402d6fa2ed2124969546d2aa58ad568e33e4cccba723873</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/7250126$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CONDÒ, Saverio G.</creatorcontrib><creatorcontrib>GIARDINA, Bruno</creatorcontrib><creatorcontrib>BARRA, Donatella</creatorcontrib><creatorcontrib>GILL, Stanley J.</creatorcontrib><creatorcontrib>BRUNORI, Maurizio</creatorcontrib><title>Purification and Functional Properties of the Hemoglobin Components from the Rat (Wistar)</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Homogeneous components of Wistar rat hemoglobin have been isolated and characterized from the molecular and functional point of view. The O2 equilibrium behaviour of the three main components (HbII, HbIII, HbIVA) has been investigated as a function of pH and organic phosphate concentration.
The ligand‐binding kinetics of the isolated components have been also studied and are fully consistent with their equilibrium behaviour. It should be remarked that the choice of the system was governed largely by the ability of rat hemoglobins to crystallize very quickly. This almost unique molecular property together with the complete reversibility of the process may allow information to be obtained on the thermodynamics of ligand linked phase changes.</description><subject>Animals</subject><subject>Hemoglobins - isolation & purification</subject><subject>Hydrogen-Ion Concentration</subject><subject>Isoelectric Focusing</subject><subject>Kinetics</subject><subject>Oxyhemoglobins - metabolism</subject><subject>Photolysis</subject><subject>Phytic Acid - pharmacology</subject><subject>Rats</subject><subject>Solubility</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE1LxDAQhoMouq7-BCF4ED205rutF9Fl1xUWFD8QTyFNU83SNmvSov57W3fx7lyG4Zl3Bh4AjjGKcV_nyxgzSiKMKI1xluK4zRGnhMdfW2D0h7bBCCHMIpJxsQf2Q1gihEQmkl2wmxCOMBEj8HrfeVtarVrrGqiaAs66Rg-DquC9dyvjW2sCdCVs3w2cm9q9VS63DZy4euUa07QBlt7Vv_hBtfD0xYZW-bMDsFOqKpjDTR-D59n0aTKPFnc3t5OrRaQZITRKcS5EhjHKC4Y1NzlmiBSiVMQUBBOWiYwzURCleKoKLlJDqWFa61wlhKYJHYOT9d2Vdx-dCa2sbdCmqlRjXBdkQrlArLcyBhfrRe1dCN6UcuVtrfy3xEgOXuVSDvLkIE8OXuXGq_zqw0ebL11em-IvuhHZ88s1_7SV-f7HZTmbXj8SRukPA2GH5A</recordid><startdate>19810515</startdate><enddate>19810515</enddate><creator>CONDÒ, Saverio G.</creator><creator>GIARDINA, Bruno</creator><creator>BARRA, Donatella</creator><creator>GILL, Stanley J.</creator><creator>BRUNORI, Maurizio</creator><general>Blackwell Publishing Ltd</general><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>19810515</creationdate><title>Purification and Functional Properties of the Hemoglobin Components from the Rat (Wistar)</title><author>CONDÒ, Saverio G. ; GIARDINA, Bruno ; BARRA, Donatella ; GILL, Stanley J. ; BRUNORI, Maurizio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4223-81b669110bd41c5eb1402d6fa2ed2124969546d2aa58ad568e33e4cccba723873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Animals</topic><topic>Hemoglobins - isolation & purification</topic><topic>Hydrogen-Ion Concentration</topic><topic>Isoelectric Focusing</topic><topic>Kinetics</topic><topic>Oxyhemoglobins - metabolism</topic><topic>Photolysis</topic><topic>Phytic Acid - pharmacology</topic><topic>Rats</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CONDÒ, Saverio G.</creatorcontrib><creatorcontrib>GIARDINA, Bruno</creatorcontrib><creatorcontrib>BARRA, Donatella</creatorcontrib><creatorcontrib>GILL, Stanley J.</creatorcontrib><creatorcontrib>BRUNORI, Maurizio</creatorcontrib><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>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CONDÒ, Saverio G.</au><au>GIARDINA, Bruno</au><au>BARRA, Donatella</au><au>GILL, Stanley J.</au><au>BRUNORI, Maurizio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Functional Properties of the Hemoglobin Components from the Rat (Wistar)</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1981-05-15</date><risdate>1981</risdate><volume>116</volume><issue>2</issue><spage>243</spage><epage>247</epage><pages>243-247</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Homogeneous components of Wistar rat hemoglobin have been isolated and characterized from the molecular and functional point of view. The O2 equilibrium behaviour of the three main components (HbII, HbIII, HbIVA) has been investigated as a function of pH and organic phosphate concentration.
The ligand‐binding kinetics of the isolated components have been also studied and are fully consistent with their equilibrium behaviour. It should be remarked that the choice of the system was governed largely by the ability of rat hemoglobins to crystallize very quickly. This almost unique molecular property together with the complete reversibility of the process may allow information to be obtained on the thermodynamics of ligand linked phase changes.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>7250126</pmid><doi>10.1111/j.1432-1033.1981.tb05325.x</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Hemoglobins - isolation & purification Hydrogen-Ion Concentration Isoelectric Focusing Kinetics Oxyhemoglobins - metabolism Photolysis Phytic Acid - pharmacology Rats Solubility |
title | Purification and Functional Properties of the Hemoglobin Components from the Rat (Wistar) |
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