The pH dependence of the inhibition of ascorbate oxidase by anions
Double-reciprocal plots of azide inhibition, with respect to ascorbate, of ascorbate oxidase indicate mixed-type inhibition at pH values above 6. This is in contrast to the simple competitive inhibition previously observed at pH 5.6. Linear replots of the slopes and intercepts of the double-reciproc...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1980-01, Vol.96 (3), p.1343-1348 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Sheline, Rebecca R. Strothkamp, Kenneth G. |
| description | Double-reciprocal plots of azide inhibition, with respect to ascorbate, of ascorbate oxidase indicate mixed-type inhibition at pH values above 6. This is in contrast to the simple competitive inhibition previously observed at pH 5.6. Linear replots of the slopes and intercepts of the double-reciprocal plots yield two inhibition constants. Both constants are pH dependent. Similar inhibition patterns are obtained with fluoride and thiocyanate. These results suggest the presence of two inhibitor binding sites, one of which is competitive with respect to ascorbate and the other uncompetitive. |
| doi_str_mv | 10.1016/0006-291X(80)90098-4 |
| format | Article |
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This is in contrast to the simple competitive inhibition previously observed at pH 5.6. Linear replots of the slopes and intercepts of the double-reciprocal plots yield two inhibition constants. Both constants are pH dependent. Similar inhibition patterns are obtained with fluoride and thiocyanate. These results suggest the presence of two inhibitor binding sites, one of which is competitive with respect to ascorbate and the other uncompetitive.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(80)90098-4</identifier><identifier>PMID: 7437074</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Anions - pharmacology ; Ascorbate Oxidase - antagonists & inhibitors ; Azides - pharmacology ; Binding Sites ; Binding, Competitive ; Fluorides - pharmacology ; Hydrogen-Ion Concentration ; Kinetics ; Oxidoreductases - antagonists & inhibitors ; Plants ; Thiocyanates - pharmacology</subject><ispartof>Biochemical and biophysical research communications, 1980-01, Vol.96 (3), p.1343-1348</ispartof><rights>1980</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-fd63df72ecb4c2d51fa2a33300ec5ec2d1704f828c80abcbb2eb0b2db1cd8bc23</citedby><cites>FETCH-LOGICAL-c357t-fd63df72ecb4c2d51fa2a33300ec5ec2d1704f828c80abcbb2eb0b2db1cd8bc23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(80)90098-4$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,778,782,3539,27907,27908,45978</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7437074$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sheline, Rebecca R.</creatorcontrib><creatorcontrib>Strothkamp, Kenneth G.</creatorcontrib><title>The pH dependence of the inhibition of ascorbate oxidase by anions</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Double-reciprocal plots of azide inhibition, with respect to ascorbate, of ascorbate oxidase indicate mixed-type inhibition at pH values above 6. This is in contrast to the simple competitive inhibition previously observed at pH 5.6. Linear replots of the slopes and intercepts of the double-reciprocal plots yield two inhibition constants. Both constants are pH dependent. Similar inhibition patterns are obtained with fluoride and thiocyanate. These results suggest the presence of two inhibitor binding sites, one of which is competitive with respect to ascorbate and the other uncompetitive.</description><subject>Anions - pharmacology</subject><subject>Ascorbate Oxidase - antagonists & inhibitors</subject><subject>Azides - pharmacology</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Fluorides - pharmacology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Oxidoreductases - antagonists & inhibitors</subject><subject>Plants</subject><subject>Thiocyanates - pharmacology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKA0EQRRtRYoz-gcKsRBej1Y95bQQNaoSAmwjumn7UkJZkeuyeiPl7Z0xwKRQU3HurijqEnFO4oUDzWwDIU1bR96sSriuAqkzFARlTqCBlFMQhGf9FjslJjB8AlIq8GpFRIXgBhRiTh8USk3aWWGyxsdgYTHyddL3omqXTrnO-GRQVjQ9adb397ayKmOhtoprejafkqFariGf7PiFvT4-L6Sydvz6_TO_nqeFZ0aW1zbmtC4ZGC8NsRmvFFOccAE2GvUILEHXJSlOC0kZrhho0s5oaW2rD-IRc7va2wX9uMHZy7aLB1Uo16DdRFhnnbKgJEbugCT7GgLVsg1ursJUU5IBODlzkwEWWIH_RSdGPXez3b_Qa7d_QnlXv3-187J_8chhkNG4gZl1A00nr3f8HfgCwJX4y</recordid><startdate>19800101</startdate><enddate>19800101</enddate><creator>Sheline, Rebecca R.</creator><creator>Strothkamp, Kenneth G.</creator><general>Elsevier Inc</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>19800101</creationdate><title>The pH dependence of the inhibition of ascorbate oxidase by anions</title><author>Sheline, Rebecca R. ; Strothkamp, Kenneth G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-fd63df72ecb4c2d51fa2a33300ec5ec2d1704f828c80abcbb2eb0b2db1cd8bc23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Anions - pharmacology</topic><topic>Ascorbate Oxidase - antagonists & inhibitors</topic><topic>Azides - pharmacology</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Fluorides - pharmacology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Oxidoreductases - antagonists & inhibitors</topic><topic>Plants</topic><topic>Thiocyanates - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sheline, Rebecca R.</creatorcontrib><creatorcontrib>Strothkamp, Kenneth G.</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sheline, Rebecca R.</au><au>Strothkamp, Kenneth G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The pH dependence of the inhibition of ascorbate oxidase by anions</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1980-01-01</date><risdate>1980</risdate><volume>96</volume><issue>3</issue><spage>1343</spage><epage>1348</epage><pages>1343-1348</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Double-reciprocal plots of azide inhibition, with respect to ascorbate, of ascorbate oxidase indicate mixed-type inhibition at pH values above 6. This is in contrast to the simple competitive inhibition previously observed at pH 5.6. Linear replots of the slopes and intercepts of the double-reciprocal plots yield two inhibition constants. Both constants are pH dependent. Similar inhibition patterns are obtained with fluoride and thiocyanate. These results suggest the presence of two inhibitor binding sites, one of which is competitive with respect to ascorbate and the other uncompetitive.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7437074</pmid><doi>10.1016/0006-291X(80)90098-4</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1980-01, Vol.96 (3), p.1343-1348 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75332332 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Anions - pharmacology Ascorbate Oxidase - antagonists & inhibitors Azides - pharmacology Binding Sites Binding, Competitive Fluorides - pharmacology Hydrogen-Ion Concentration Kinetics Oxidoreductases - antagonists & inhibitors Plants Thiocyanates - pharmacology |
| title | The pH dependence of the inhibition of ascorbate oxidase by anions |
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