The allosteric effect of inositol hexasulfate on oxygen binding by hemoglobin

Myoinositol hexasulfate (IHS) is a powerful allosteric effector of oxygen binding by hemoglobin. It binds to deoxyhemoglobin at the same site as 2,3-diphosphoglycerate (DPG) and inositol hexaphosphate (IHP) with an affinity which is intermediate between that of the two phosphate esters. The binding...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Easton) 1976-07, Vol.15 (15), p.3396-3398
Main Authors: Benesch, Reinhold, Edalji, Rohinton, Benesch, Ruth E
Format: Article
Language:English
Subjects:
Binding Sites
Diphosphoglyceric Acids - pharmacology
Dose-Response Relationship, Drug
Hemoglobins - metabolism
Humans
Inositol - pharmacology
Oxygen - metabolism
Phytic Acid - pharmacology
Protein Binding
Sulfuric Acids - pharmacology
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-a353t-bb21490f73e4f8ccbb8fc5a09c3076ebf51730de665506e59cbbeaebf21fbe23
cites
container_end_page 3398
container_issue 15
container_start_page 3396
container_title Biochemistry (Easton)
container_volume 15
creator Benesch, Reinhold
Edalji, Rohinton
Benesch, Ruth E
description Myoinositol hexasulfate (IHS) is a powerful allosteric effector of oxygen binding by hemoglobin. It binds to deoxyhemoglobin at the same site as 2,3-diphosphoglycerate (DPG) and inositol hexaphosphate (IHP) with an affinity which is intermediate between that of the two phosphate esters. The binding constant calculated from the displacement of the oxygenation curve in the presence of low concentrations of IHS is 0.9X10(6) M. The value obtained directly from the number of protons bound as a function of IHS concentration is 1.0X10(6) M. The agreement between these two independent measurements provides an experimental verification of the empirical equation, relating the oxygen affinity to the binding constants, proposed previously (Benesch, R.E., Benesch, R., Renthal, R and Gratzer, W.B. (1971), Nature (London), New Biol. 2348 174).
doi_str_mv 10.1021/bi00660a035
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_83488291</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>83488291</sourcerecordid><originalsourceid>FETCH-LOGICAL-a353t-bb21490f73e4f8ccbb8fc5a09c3076ebf51730de665506e59cbbeaebf21fbe23</originalsourceid><addsrcrecordid>eNptkM9LwzAUx4P4a05PXj3kpAepJk2TtkcVp8KGigPBS0iylxntGm1a2P57Ix3Dg6fHe98P3wcfhI4puaAkpZfaESIEUYTxLTSgPCVJVpZ8Gw1IDJK0FGQfHYTwEdeM5Nke2i15Wgg2QJPpO2BVVT600DiDwVowLfYWu9oH1_oKv8NSha6yqgXsa-yXqznUWLt65uo51qsILPy88vFyiHasqgIcrecQTUe305v7ZPx493BzNU4U46xNtE5pVhKbM8hsYYzWhTVckdIwkgvQltOckRkIwTkRwMtIgIr3lFoNKRui0772q_HfHYRWLlwwUFWqBt8FWbCsKNKSRvC8B03jQ2jAyq_GLVSzkpTIX3Xyj7pIn6xrO72A2YbtXcU46WMXXS03qWo-pchZzuX06UWOnjl9u85f5STyZz2vTJAfvmvqqOTfxz-zSIXk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83488291</pqid></control><display><type>article</type><title>The allosteric effect of inositol hexasulfate on oxygen binding by hemoglobin</title><source>ACS CRKN Legacy Archives</source><creator>Benesch, Reinhold ; Edalji, Rohinton ; Benesch, Ruth E</creator><creatorcontrib>Benesch, Reinhold ; Edalji, Rohinton ; Benesch, Ruth E</creatorcontrib><description>Myoinositol hexasulfate (IHS) is a powerful allosteric effector of oxygen binding by hemoglobin. It binds to deoxyhemoglobin at the same site as 2,3-diphosphoglycerate (DPG) and inositol hexaphosphate (IHP) with an affinity which is intermediate between that of the two phosphate esters. The binding constant calculated from the displacement of the oxygenation curve in the presence of low concentrations of IHS is 0.9X10(6) M. The value obtained directly from the number of protons bound as a function of IHS concentration is 1.0X10(6) M. The agreement between these two independent measurements provides an experimental verification of the empirical equation, relating the oxygen affinity to the binding constants, proposed previously (Benesch, R.E., Benesch, R., Renthal, R and Gratzer, W.B. (1971), Nature (London), New Biol. 2348 174).</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00660a035</identifier><identifier>PMID: 952863</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Binding Sites ; Diphosphoglyceric Acids - pharmacology ; Dose-Response Relationship, Drug ; Hemoglobins - metabolism ; Humans ; Inositol - pharmacology ; Oxygen - metabolism ; Phytic Acid - pharmacology ; Protein Binding ; Sulfuric Acids - pharmacology</subject><ispartof>Biochemistry (Easton), 1976-07, Vol.15 (15), p.3396-3398</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a353t-bb21490f73e4f8ccbb8fc5a09c3076ebf51730de665506e59cbbeaebf21fbe23</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/bi00660a035$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00660a035$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,27064,27924,27925,56766,56816</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/952863$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Benesch, Reinhold</creatorcontrib><creatorcontrib>Edalji, Rohinton</creatorcontrib><creatorcontrib>Benesch, Ruth E</creatorcontrib><title>The allosteric effect of inositol hexasulfate on oxygen binding by hemoglobin</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Myoinositol hexasulfate (IHS) is a powerful allosteric effector of oxygen binding by hemoglobin. It binds to deoxyhemoglobin at the same site as 2,3-diphosphoglycerate (DPG) and inositol hexaphosphate (IHP) with an affinity which is intermediate between that of the two phosphate esters. The binding constant calculated from the displacement of the oxygenation curve in the presence of low concentrations of IHS is 0.9X10(6) M. The value obtained directly from the number of protons bound as a function of IHS concentration is 1.0X10(6) M. The agreement between these two independent measurements provides an experimental verification of the empirical equation, relating the oxygen affinity to the binding constants, proposed previously (Benesch, R.E., Benesch, R., Renthal, R and Gratzer, W.B. (1971), Nature (London), New Biol. 2348 174).</description><subject>Binding Sites</subject><subject>Diphosphoglyceric Acids - pharmacology</subject><subject>Dose-Response Relationship, Drug</subject><subject>Hemoglobins - metabolism</subject><subject>Humans</subject><subject>Inositol - pharmacology</subject><subject>Oxygen - metabolism</subject><subject>Phytic Acid - pharmacology</subject><subject>Protein Binding</subject><subject>Sulfuric Acids - pharmacology</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1976</creationdate><recordtype>article</recordtype><recordid>eNptkM9LwzAUx4P4a05PXj3kpAepJk2TtkcVp8KGigPBS0iylxntGm1a2P57Ix3Dg6fHe98P3wcfhI4puaAkpZfaESIEUYTxLTSgPCVJVpZ8Gw1IDJK0FGQfHYTwEdeM5Nke2i15Wgg2QJPpO2BVVT600DiDwVowLfYWu9oH1_oKv8NSha6yqgXsa-yXqznUWLt65uo51qsILPy88vFyiHasqgIcrecQTUe305v7ZPx493BzNU4U46xNtE5pVhKbM8hsYYzWhTVckdIwkgvQltOckRkIwTkRwMtIgIr3lFoNKRui0772q_HfHYRWLlwwUFWqBt8FWbCsKNKSRvC8B03jQ2jAyq_GLVSzkpTIX3Xyj7pIn6xrO72A2YbtXcU46WMXXS03qWo-pchZzuX06UWOnjl9u85f5STyZz2vTJAfvmvqqOTfxz-zSIXk</recordid><startdate>19760727</startdate><enddate>19760727</enddate><creator>Benesch, Reinhold</creator><creator>Edalji, Rohinton</creator><creator>Benesch, Ruth E</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>7X8</scope></search><sort><creationdate>19760727</creationdate><title>The allosteric effect of inositol hexasulfate on oxygen binding by hemoglobin</title><author>Benesch, Reinhold ; Edalji, Rohinton ; Benesch, Ruth E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a353t-bb21490f73e4f8ccbb8fc5a09c3076ebf51730de665506e59cbbeaebf21fbe23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1976</creationdate><topic>Binding Sites</topic><topic>Diphosphoglyceric Acids - pharmacology</topic><topic>Dose-Response Relationship, Drug</topic><topic>Hemoglobins - metabolism</topic><topic>Humans</topic><topic>Inositol - pharmacology</topic><topic>Oxygen - metabolism</topic><topic>Phytic Acid - pharmacology</topic><topic>Protein Binding</topic><topic>Sulfuric Acids - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Benesch, Reinhold</creatorcontrib><creatorcontrib>Edalji, Rohinton</creatorcontrib><creatorcontrib>Benesch, Ruth E</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>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Benesch, Reinhold</au><au>Edalji, Rohinton</au><au>Benesch, Ruth E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The allosteric effect of inositol hexasulfate on oxygen binding by hemoglobin</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1976-07-27</date><risdate>1976</risdate><volume>15</volume><issue>15</issue><spage>3396</spage><epage>3398</epage><pages>3396-3398</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Myoinositol hexasulfate (IHS) is a powerful allosteric effector of oxygen binding by hemoglobin. It binds to deoxyhemoglobin at the same site as 2,3-diphosphoglycerate (DPG) and inositol hexaphosphate (IHP) with an affinity which is intermediate between that of the two phosphate esters. The binding constant calculated from the displacement of the oxygenation curve in the presence of low concentrations of IHS is 0.9X10(6) M. The value obtained directly from the number of protons bound as a function of IHS concentration is 1.0X10(6) M. The agreement between these two independent measurements provides an experimental verification of the empirical equation, relating the oxygen affinity to the binding constants, proposed previously (Benesch, R.E., Benesch, R., Renthal, R and Gratzer, W.B. (1971), Nature (London), New Biol. 2348 174).</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>952863</pmid><doi>10.1021/bi00660a035</doi><tpages>3</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-2960
ispartof Biochemistry (Easton), 1976-07, Vol.15 (15), p.3396-3398
issn 0006-2960
1520-4995
language eng
recordid cdi_proquest_miscellaneous_83488291
source ACS CRKN Legacy Archives
subjects Binding Sites
Diphosphoglyceric Acids - pharmacology
Dose-Response Relationship, Drug
Hemoglobins - metabolism
Humans
Inositol - pharmacology
Oxygen - metabolism
Phytic Acid - pharmacology
Protein Binding
Sulfuric Acids - pharmacology
title The allosteric effect of inositol hexasulfate on oxygen binding by hemoglobin
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-30T20%3A11%3A09IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20allosteric%20effect%20of%20inositol%20hexasulfate%20on%20oxygen%20binding%20by%20hemoglobin&rft.jtitle=Biochemistry%20(Easton)&rft.au=Benesch,%20Reinhold&rft.date=1976-07-27&rft.volume=15&rft.issue=15&rft.spage=3396&rft.epage=3398&rft.pages=3396-3398&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi00660a035&rft_dat=%3Cproquest_cross%3E83488291%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a353t-bb21490f73e4f8ccbb8fc5a09c3076ebf51730de665506e59cbbeaebf21fbe23%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=83488291&rft_id=info:pmid/952863&rfr_iscdi=true