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Observations on the Kinetics of the Reaction of Hemoglobin with Oxygen
The kinetics of the reaction of human deoxyhemoglobin with oxygen at high concentrations of ligand (â¼10 -4 m ) has been studied with the use of a fast stopped flow apparatus with a dead time of approximately 300 µsec. The shape of the progress curve reveals that the apparent second order rate con...
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Published in: | The Journal of biological chemistry 1967-10, Vol.242 (20), p.4841-4843 |
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container_end_page | 4843 |
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container_title | The Journal of biological chemistry |
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creator | Berger, Robert L. Antonini, Eraldo Brunori, Maurizio Wyman, Jeffries Rossi-Fanelli, Alessandro |
description | The kinetics of the reaction of human deoxyhemoglobin with oxygen at high concentrations of ligand (â¼10 -4 m ) has been studied with the use of a fast stopped flow apparatus with a dead time of approximately 300 µsec. The shape of
the progress curve reveals that the apparent second order rate constant for the reaction with oxygen ( k ') increases with the extent of the reaction, similar to what was reported for other ligands ( i.e. carbon monoxide). Within the oxygen concentration range studied, the rate of the reaction at any stage is proportional to
the ligand concentration, notwithstanding the change in rate as the reaction proceeds.
These results are interpreted to indicate that the ligand-linked intramolecular change in hemoglobin is a fast process which
occurs in a fraction of a millisecond. |
doi_str_mv | 10.1016/S0021-9258(18)99532-3 |
format | article |
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the progress curve reveals that the apparent second order rate constant for the reaction with oxygen ( k ') increases with the extent of the reaction, similar to what was reported for other ligands ( i.e. carbon monoxide). Within the oxygen concentration range studied, the rate of the reaction at any stage is proportional to
the ligand concentration, notwithstanding the change in rate as the reaction proceeds.
These results are interpreted to indicate that the ligand-linked intramolecular change in hemoglobin is a fast process which
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the progress curve reveals that the apparent second order rate constant for the reaction with oxygen ( k ') increases with the extent of the reaction, similar to what was reported for other ligands ( i.e. carbon monoxide). Within the oxygen concentration range studied, the rate of the reaction at any stage is proportional to
the ligand concentration, notwithstanding the change in rate as the reaction proceeds.
These results are interpreted to indicate that the ligand-linked intramolecular change in hemoglobin is a fast process which
occurs in a fraction of a millisecond.</description><subject>Hemoglobins</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Oscillometry</subject><subject>Oxygen</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1967</creationdate><recordtype>article</recordtype><recordid>eNo9kFtLw0AQhRdRtFZ_ghAQRB-iO3vr7qMUa0Wh4AV8WzbZabPSJDWbWv33phc6L8PhnLnwEXIB9BYoqLs3Shmkhkl9DfrGGMlZyg9ID6jmKZfweUh6-8gJOY3xi3YlDByTY0UVCCZ7ZDTJIjY_rg11FZO6StoCk-dQYRvyTk83-hVdvg6s9RjLejavs1Alq9AWyeT3b4bVGTmaunnE813vk4_Rw_twnL5MHp-G9y9pzgemTb03noEaoPNCAxoOSngUwnvJpOfdp74zp0ajRJMpL9Fp4CofaOc4ZIz3ydV276Kpv5cYW1uGmON87iqsl9FqoYAqZbqg3Abzpo6xwaldNKF0zZ8Fatf87IafXcOxoO2Gn-Xd3MXuwDIr0e-ndsA6_3LrF2FWrEKDNgt1XmBpmWCWUSu0AP4PEYp2rw</recordid><startdate>19671025</startdate><enddate>19671025</enddate><creator>Berger, Robert L.</creator><creator>Antonini, Eraldo</creator><creator>Brunori, Maurizio</creator><creator>Wyman, Jeffries</creator><creator>Rossi-Fanelli, Alessandro</creator><general>American Society for Biochemistry and Molecular Biology</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>19671025</creationdate><title>Observations on the Kinetics of the Reaction of Hemoglobin with Oxygen</title><author>Berger, Robert L. ; Antonini, Eraldo ; Brunori, Maurizio ; Wyman, Jeffries ; Rossi-Fanelli, Alessandro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-dd9d2167ead481e93164de44dd525d3925d67ef98e5e9b6d5ea8136c78aa31b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1967</creationdate><topic>Hemoglobins</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Oscillometry</topic><topic>Oxygen</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Berger, Robert L.</creatorcontrib><creatorcontrib>Antonini, Eraldo</creatorcontrib><creatorcontrib>Brunori, Maurizio</creatorcontrib><creatorcontrib>Wyman, Jeffries</creatorcontrib><creatorcontrib>Rossi-Fanelli, Alessandro</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Berger, Robert L.</au><au>Antonini, Eraldo</au><au>Brunori, Maurizio</au><au>Wyman, Jeffries</au><au>Rossi-Fanelli, Alessandro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Observations on the Kinetics of the Reaction of Hemoglobin with Oxygen</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1967-10-25</date><risdate>1967</risdate><volume>242</volume><issue>20</issue><spage>4841</spage><epage>4843</epage><pages>4841-4843</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The kinetics of the reaction of human deoxyhemoglobin with oxygen at high concentrations of ligand (â¼10 -4 m ) has been studied with the use of a fast stopped flow apparatus with a dead time of approximately 300 µsec. The shape of
the progress curve reveals that the apparent second order rate constant for the reaction with oxygen ( k ') increases with the extent of the reaction, similar to what was reported for other ligands ( i.e. carbon monoxide). Within the oxygen concentration range studied, the rate of the reaction at any stage is proportional to
the ligand concentration, notwithstanding the change in rate as the reaction proceeds.
These results are interpreted to indicate that the ligand-linked intramolecular change in hemoglobin is a fast process which
occurs in a fraction of a millisecond.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6061425</pmid><doi>10.1016/S0021-9258(18)99532-3</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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source | ScienceDirect Journals |
subjects | Hemoglobins Humans Kinetics Oscillometry Oxygen |
title | Observations on the Kinetics of the Reaction of Hemoglobin with Oxygen |
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