Kinetics of carbon monoxide and oxygen binding for eight electrophoretic components of sperm-whale myoglobin
Sperm-whale myoglobin has been fractionated by isoelectric focusing in Sephadex gels, and O sub(2) and CO ligand association and dissociation kinetics were measured by stopped-flow and flash photolysis for the 8 most abundant fractions. Except for the association rate for CO binding, there appeared...
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| Veröffentlicht in: | Biochemistry (Easton) 1972-11, Vol.11 (24), p.4520-4525 |
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| container_title | Biochemistry (Easton) |
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| creator | LaGow, Joyce Parkhurst, Lawrence J |
| description | Sperm-whale myoglobin has been fractionated by isoelectric focusing in Sephadex gels, and O sub(2) and CO ligand association and dissociation kinetics were measured by stopped-flow and flash photolysis for the 8 most abundant fractions. Except for the association rate for CO binding, there appeared to be no significant differences in rates among the various bands for a given reaction. Rates for O sub(2) dissociation and association determined by replacement reactions were in good agreement with rates determined with dithionite and by flash photolysis, respectively. The rate for CO dissociation determined by NO replacement was homogeneous. Heterogeneous kinetics were observed for the dissociation reaction when Fe(CN) sub(6) super(3-) was used. An evaluation of M, the O sub(2) super(-) CO partition constant, from the kinetic data was in excellent agreement with a direct equilibrium determination. |
| doi_str_mv | 10.1021/bi00774a014 |
| format | Article |
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Except for the association rate for CO binding, there appeared to be no significant differences in rates among the various bands for a given reaction. Rates for O sub(2) dissociation and association determined by replacement reactions were in good agreement with rates determined with dithionite and by flash photolysis, respectively. The rate for CO dissociation determined by NO replacement was homogeneous. Heterogeneous kinetics were observed for the dissociation reaction when Fe(CN) sub(6) super(3-) was used. An evaluation of M, the O sub(2) super(-) CO partition constant, from the kinetic data was in excellent agreement with a direct equilibrium determination.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00774a014</identifier><identifier>PMID: 4675876</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Carbon Monoxide ; Cetacea ; Chromatography, Gel ; Ferricyanides ; Isoelectric Focusing ; Kinetics ; Marine ; Mathematics ; Myoglobin ; Nitric Oxide ; Oxygen ; Photolysis ; Protein Binding ; Spectrophotometry ; Sulfites</subject><ispartof>Biochemistry (Easton), 1972-11, Vol.11 (24), p.4520-4525</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a317t-19ffa572f6b3619ad32d7e0ae349266044e28f912c5e1c0c591b5177b2bdbb4c3</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/bi00774a014$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00774a014$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4675876$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LaGow, Joyce</creatorcontrib><creatorcontrib>Parkhurst, Lawrence J</creatorcontrib><title>Kinetics of carbon monoxide and oxygen binding for eight electrophoretic components of sperm-whale myoglobin</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Sperm-whale myoglobin has been fractionated by isoelectric focusing in Sephadex gels, and O sub(2) and CO ligand association and dissociation kinetics were measured by stopped-flow and flash photolysis for the 8 most abundant fractions. Except for the association rate for CO binding, there appeared to be no significant differences in rates among the various bands for a given reaction. Rates for O sub(2) dissociation and association determined by replacement reactions were in good agreement with rates determined with dithionite and by flash photolysis, respectively. The rate for CO dissociation determined by NO replacement was homogeneous. Heterogeneous kinetics were observed for the dissociation reaction when Fe(CN) sub(6) super(3-) was used. An evaluation of M, the O sub(2) super(-) CO partition constant, from the kinetic data was in excellent agreement with a direct equilibrium determination.</description><subject>Animals</subject><subject>Carbon Monoxide</subject><subject>Cetacea</subject><subject>Chromatography, Gel</subject><subject>Ferricyanides</subject><subject>Isoelectric Focusing</subject><subject>Kinetics</subject><subject>Marine</subject><subject>Mathematics</subject><subject>Myoglobin</subject><subject>Nitric Oxide</subject><subject>Oxygen</subject><subject>Photolysis</subject><subject>Protein Binding</subject><subject>Spectrophotometry</subject><subject>Sulfites</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1972</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1rGzEQhkVISZ20p5wLOjWHsq2k1Yd1DCEfJYamNO1VSNpZW8mutJHW1P733dQm9FDIaRjeh2dgXoROKflMCaNfXCBEKW4J5QdoRgUjFddaHKIZIURWTEvyFh2X8jCtnCh-hI64VGKu5Ax1tyHCGHzBqcXeZpci7lNMm9AAtrHBabNdQsQuxCbEJW5TxhCWqxFDB37MaVil_CzAPvVDihDHv6oyQO6r3yvbAe63admlyfAOvWltV-D9fp6gn1eX9xc31eLb9deL80Vla6rGiuq2tUKxVrpaUm2bmjUKiIWaayYl4RzYvNWUeQHUEy80dYIq5ZhrnOO-PkEfd94hp6c1lNH0oXjoOhshrYuZUzXhgr4KUqWp4lJP4Kcd6HMqJUNrhhx6m7eGEvNcgvmnhIn-sNeuXQ_NC7v_-pRXuzyUETYvsc2PRqpaCXN_98Nc_bq9-764ZkZN_NmOt76Yh7TOcfrefy__AaTxnu0</recordid><startdate>19721101</startdate><enddate>19721101</enddate><creator>LaGow, Joyce</creator><creator>Parkhurst, Lawrence J</creator><general>American Chemical Society</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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19721101</creationdate><title>Kinetics of carbon monoxide and oxygen binding for eight electrophoretic components of sperm-whale myoglobin</title><author>LaGow, Joyce ; Parkhurst, Lawrence J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a317t-19ffa572f6b3619ad32d7e0ae349266044e28f912c5e1c0c591b5177b2bdbb4c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1972</creationdate><topic>Animals</topic><topic>Carbon Monoxide</topic><topic>Cetacea</topic><topic>Chromatography, Gel</topic><topic>Ferricyanides</topic><topic>Isoelectric Focusing</topic><topic>Kinetics</topic><topic>Marine</topic><topic>Mathematics</topic><topic>Myoglobin</topic><topic>Nitric Oxide</topic><topic>Oxygen</topic><topic>Photolysis</topic><topic>Protein Binding</topic><topic>Spectrophotometry</topic><topic>Sulfites</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LaGow, Joyce</creatorcontrib><creatorcontrib>Parkhurst, Lawrence J</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>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><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LaGow, Joyce</au><au>Parkhurst, Lawrence J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics of carbon monoxide and oxygen binding for eight electrophoretic components of sperm-whale myoglobin</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1972-11-01</date><risdate>1972</risdate><volume>11</volume><issue>24</issue><spage>4520</spage><epage>4525</epage><pages>4520-4525</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Sperm-whale myoglobin has been fractionated by isoelectric focusing in Sephadex gels, and O sub(2) and CO ligand association and dissociation kinetics were measured by stopped-flow and flash photolysis for the 8 most abundant fractions. Except for the association rate for CO binding, there appeared to be no significant differences in rates among the various bands for a given reaction. Rates for O sub(2) dissociation and association determined by replacement reactions were in good agreement with rates determined with dithionite and by flash photolysis, respectively. The rate for CO dissociation determined by NO replacement was homogeneous. Heterogeneous kinetics were observed for the dissociation reaction when Fe(CN) sub(6) super(3-) was used. An evaluation of M, the O sub(2) super(-) CO partition constant, from the kinetic data was in excellent agreement with a direct equilibrium determination.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>4675876</pmid><doi>10.1021/bi00774a014</doi><tpages>6</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | Animals Carbon Monoxide Cetacea Chromatography, Gel Ferricyanides Isoelectric Focusing Kinetics Marine Mathematics Myoglobin Nitric Oxide Oxygen Photolysis Protein Binding Spectrophotometry Sulfites |
| title | Kinetics of carbon monoxide and oxygen binding for eight electrophoretic components of sperm-whale myoglobin |
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