Structural specificities in acylation of hemoglobin and sickle hemoglobin by diaspirins
Double-headed aspirins with bridging groups of different length and molecular structure have been examined for their reactivity with hemoglobin A or S. The compounds constructed are bound in the beta-cleft and show a wide range of beta-beta cross-linking effectiveness. Oxygenation curves of the modi...
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| Veröffentlicht in: | The Journal of biological chemistry 1981-07, Vol.256 (13), p.7046-7052 |
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| container_end_page | 7052 |
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| container_issue | 13 |
| container_start_page | 7046 |
| container_title | The Journal of biological chemistry |
| container_volume | 256 |
| creator | Wood, L E Haney, D N Patel, J R Clare, S E Shi, G Y King, L C Klotz, I M |
| description | Double-headed aspirins with bridging groups of different length and molecular structure have been examined for their reactivity
with hemoglobin A or S. The compounds constructed are bound in the beta-cleft and show a wide range of beta-beta cross-linking
effectiveness. Oxygenation curves of the modified hemoglobins in the presence of inositol hexaphosphate are strikingly modified.
Many of the diaspirins also produce substantial changes in the minimum gelling concentration of sickle hemoglobin. These reagents
offer possibilities for further enhancement of specificity toward hemoglobin, particularly by taking advantage of stereoselectivities. |
| doi_str_mv | 10.1016/S0021-9258(19)69097-6 |
| format | Article |
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with hemoglobin A or S. The compounds constructed are bound in the beta-cleft and show a wide range of beta-beta cross-linking
effectiveness. Oxygenation curves of the modified hemoglobins in the presence of inositol hexaphosphate are strikingly modified.
Many of the diaspirins also produce substantial changes in the minimum gelling concentration of sickle hemoglobin. These reagents
offer possibilities for further enhancement of specificity toward hemoglobin, particularly by taking advantage of stereoselectivities.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)69097-6</identifier><identifier>PMID: 7240262</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>aggregation ; Aspirin - analogs & derivatives ; Aspirin - chemical synthesis ; cross-linking ; Cross-Linking Reagents ; diaspirins ; hemoglobin A ; Hemoglobin A - metabolism ; hemoglobin S ; Hemoglobin, Sickle - metabolism ; Humans ; Indicators and Reagents ; man ; Methods ; oxygen ; Oxyhemoglobins - metabolism ; Protein Binding ; Structure-Activity Relationship</subject><ispartof>The Journal of biological chemistry, 1981-07, Vol.256 (13), p.7046-7052</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c410t-a3a802d4147c19c9b43604b30f7d0b5e40da14940770b3abc148f3fcd2f6c7a73</citedby><cites>FETCH-LOGICAL-c410t-a3a802d4147c19c9b43604b30f7d0b5e40da14940770b3abc148f3fcd2f6c7a73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7240262$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wood, L E</creatorcontrib><creatorcontrib>Haney, D N</creatorcontrib><creatorcontrib>Patel, J R</creatorcontrib><creatorcontrib>Clare, S E</creatorcontrib><creatorcontrib>Shi, G Y</creatorcontrib><creatorcontrib>King, L C</creatorcontrib><creatorcontrib>Klotz, I M</creatorcontrib><title>Structural specificities in acylation of hemoglobin and sickle hemoglobin by diaspirins</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Double-headed aspirins with bridging groups of different length and molecular structure have been examined for their reactivity
with hemoglobin A or S. The compounds constructed are bound in the beta-cleft and show a wide range of beta-beta cross-linking
effectiveness. Oxygenation curves of the modified hemoglobins in the presence of inositol hexaphosphate are strikingly modified.
Many of the diaspirins also produce substantial changes in the minimum gelling concentration of sickle hemoglobin. These reagents
offer possibilities for further enhancement of specificity toward hemoglobin, particularly by taking advantage of stereoselectivities.</description><subject>aggregation</subject><subject>Aspirin - analogs & derivatives</subject><subject>Aspirin - chemical synthesis</subject><subject>cross-linking</subject><subject>Cross-Linking Reagents</subject><subject>diaspirins</subject><subject>hemoglobin A</subject><subject>Hemoglobin A - metabolism</subject><subject>hemoglobin S</subject><subject>Hemoglobin, Sickle - metabolism</subject><subject>Humans</subject><subject>Indicators and Reagents</subject><subject>man</subject><subject>Methods</subject><subject>oxygen</subject><subject>Oxyhemoglobins - metabolism</subject><subject>Protein Binding</subject><subject>Structure-Activity Relationship</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMoun78BKEgiB6qM0maNEcRv0DwoKK3kKSpG-22a9Ii--_tuot4cy4D8z4zAw8hhwhnCCjOHwEo5ooW5QmqU6FAyVxskAlCyXJW4OsmmfwiO2Q3pXcYiyvcJtuScqCCTsjLYx8H1w_RNFmaexfq4EIffMpCmxm3aEwfujbr6mzqZ91b09nlvK2yFNxH4_9O7SKrgknzEEOb9slWbZrkD9Z9jzxfXz1d3ub3Dzd3lxf3ueMIfW6YKYFWHLl0qJyynAnglkEtK7CF51AZ5IqDlGCZsQ55WbPaVbQWThrJ9sjx6u48dp-DT72eheR805jWd0PSshCloKL8F8SCSTaiI1isQBe7lKKv9TyGmYkLjaCX5vWPeb3UqlHpH_NajHuH6weDnfnqd2utesyPVvk0vE2_QvTahs6N_jQthEamJXDBvgGK5Isd</recordid><startdate>19810710</startdate><enddate>19810710</enddate><creator>Wood, L E</creator><creator>Haney, D N</creator><creator>Patel, J R</creator><creator>Clare, S E</creator><creator>Shi, G Y</creator><creator>King, L C</creator><creator>Klotz, I M</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19810710</creationdate><title>Structural specificities in acylation of hemoglobin and sickle hemoglobin by diaspirins</title><author>Wood, L E ; Haney, D N ; Patel, J R ; Clare, S E ; Shi, G Y ; King, L C ; Klotz, I M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c410t-a3a802d4147c19c9b43604b30f7d0b5e40da14940770b3abc148f3fcd2f6c7a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>aggregation</topic><topic>Aspirin - analogs & derivatives</topic><topic>Aspirin - chemical synthesis</topic><topic>cross-linking</topic><topic>Cross-Linking Reagents</topic><topic>diaspirins</topic><topic>hemoglobin A</topic><topic>Hemoglobin A - metabolism</topic><topic>hemoglobin S</topic><topic>Hemoglobin, Sickle - metabolism</topic><topic>Humans</topic><topic>Indicators and Reagents</topic><topic>man</topic><topic>Methods</topic><topic>oxygen</topic><topic>Oxyhemoglobins - metabolism</topic><topic>Protein Binding</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wood, L E</creatorcontrib><creatorcontrib>Haney, D N</creatorcontrib><creatorcontrib>Patel, J R</creatorcontrib><creatorcontrib>Clare, S E</creatorcontrib><creatorcontrib>Shi, G Y</creatorcontrib><creatorcontrib>King, L C</creatorcontrib><creatorcontrib>Klotz, I M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</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>Wood, L E</au><au>Haney, D N</au><au>Patel, J R</au><au>Clare, S E</au><au>Shi, G Y</au><au>King, L C</au><au>Klotz, I M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural specificities in acylation of hemoglobin and sickle hemoglobin by diaspirins</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1981-07-10</date><risdate>1981</risdate><volume>256</volume><issue>13</issue><spage>7046</spage><epage>7052</epage><pages>7046-7052</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Double-headed aspirins with bridging groups of different length and molecular structure have been examined for their reactivity
with hemoglobin A or S. The compounds constructed are bound in the beta-cleft and show a wide range of beta-beta cross-linking
effectiveness. Oxygenation curves of the modified hemoglobins in the presence of inositol hexaphosphate are strikingly modified.
Many of the diaspirins also produce substantial changes in the minimum gelling concentration of sickle hemoglobin. These reagents
offer possibilities for further enhancement of specificity toward hemoglobin, particularly by taking advantage of stereoselectivities.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>7240262</pmid><doi>10.1016/S0021-9258(19)69097-6</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | The Journal of biological chemistry, 1981-07, Vol.256 (13), p.7046-7052 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75686268 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | aggregation Aspirin - analogs & derivatives Aspirin - chemical synthesis cross-linking Cross-Linking Reagents diaspirins hemoglobin A Hemoglobin A - metabolism hemoglobin S Hemoglobin, Sickle - metabolism Humans Indicators and Reagents man Methods oxygen Oxyhemoglobins - metabolism Protein Binding Structure-Activity Relationship |
| title | Structural specificities in acylation of hemoglobin and sickle hemoglobin by diaspirins |
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