A comparison of drug binding sites on mammalian albumins
The fluorescent probes warfarin and dansylsarcosine are known to selectively interact with binding sites I and II, respectively, on human albumin. This paper investigates whether similar binding sites exist on bovine, dog, horse, sheep and rat albumins. Binding sites on albumins were studied by: (1)...
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| Veröffentlicht in: | Biochemical pharmacology 1992-09, Vol.44 (5), p.873-879 |
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| creator | Panjehshahin, Mohammad R. Yates, Michael S. Bowmer, Christopher J. |
| description | The fluorescent probes warfarin and dansylsarcosine are known to selectively interact with binding sites I and II, respectively, on human albumin. This paper investigates whether similar binding sites exist on bovine, dog, horse, sheep and rat albumins. Binding sites on albumins were studied by: (1) displacement of warfarin and dansylsarcosine by site I (phenylbutazone) and site II (diazepam) selective ligands; (2) the effects of non-esterified fatty acids (carbon chain lengths: C
5C-
20) and changes in pH (6–9) on the fluorescence of warfarin and dansylsarcosine; and (3) the ability of site selective ligands to inhibit hydrolysis of 4-nitrophenyl acetate. For bovine, dog, horse, human and sheep albumins the fluorescence of bound warfarin and dansylsarcosine was selectively decreased by phenylbutazone and diazepam, respectively. For these albumins medium chain fatty acids (C
7-C
12) reduced the fluorescence of dansylsarcosine (maximum inhibition with C
9) whereas long chain acids (C
12-C
20) enhanced the fluorescence of warfarin (maximum increases with C
12). In addition, changes in pH from 6 to 9 increased the fluorescence of warfarin and although site I ligands (warfarin/phenylbutazone) had no pronounced effects on 4-nitrophenyl acetate hydrolysis, site II ligands (dansylsareosine/diazepam) significantly inhibited this reaction. Rat albumin behaved differently from the other albumins studied in that the C
12-C
20 fatty acids and changes in pH did not enhance the fluorescence of warfarin. Moreover, the differential effects of site I and site II ligands on the fluorescence of warfarin/dansylsarcosine and hydrolysis of 4-nitrophenyl acetate were less apparent with rat albumin. The results suggest bovine, dog, horse and sheep albumins have binding sites for warfarin and dansylsarcosine with similar properties to sites I and II on human albumin. By contrast, the warfarin binding site and to a lesser degree the dansylsarcosine site, of rat albumin have different characteristics from these sites on the other albumins studied. |
| doi_str_mv | 10.1016/0006-2952(92)90118-3 |
| format | Article |
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5C-
20) and changes in pH (6–9) on the fluorescence of warfarin and dansylsarcosine; and (3) the ability of site selective ligands to inhibit hydrolysis of 4-nitrophenyl acetate. For bovine, dog, horse, human and sheep albumins the fluorescence of bound warfarin and dansylsarcosine was selectively decreased by phenylbutazone and diazepam, respectively. For these albumins medium chain fatty acids (C
7-C
12) reduced the fluorescence of dansylsarcosine (maximum inhibition with C
9) whereas long chain acids (C
12-C
20) enhanced the fluorescence of warfarin (maximum increases with C
12). In addition, changes in pH from 6 to 9 increased the fluorescence of warfarin and although site I ligands (warfarin/phenylbutazone) had no pronounced effects on 4-nitrophenyl acetate hydrolysis, site II ligands (dansylsareosine/diazepam) significantly inhibited this reaction. Rat albumin behaved differently from the other albumins studied in that the C
12-C
20 fatty acids and changes in pH did not enhance the fluorescence of warfarin. Moreover, the differential effects of site I and site II ligands on the fluorescence of warfarin/dansylsarcosine and hydrolysis of 4-nitrophenyl acetate were less apparent with rat albumin. The results suggest bovine, dog, horse and sheep albumins have binding sites for warfarin and dansylsarcosine with similar properties to sites I and II on human albumin. By contrast, the warfarin binding site and to a lesser degree the dansylsarcosine site, of rat albumin have different characteristics from these sites on the other albumins studied.</description><identifier>ISSN: 0006-2952</identifier><identifier>EISSN: 1873-2968</identifier><identifier>DOI: 10.1016/0006-2952(92)90118-3</identifier><identifier>PMID: 1382424</identifier><identifier>CODEN: BCPCA6</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Albumins - chemistry ; Animals ; Binding Sites ; Binding, Competitive ; Biological and medical sciences ; Cattle ; Dansyl Compounds - chemistry ; Diazepam - chemistry ; Diazepam - pharmacology ; Dogs ; Fatty Acids, Nonesterified - pharmacology ; Fluorescence ; General pharmacology ; Horses ; Humans ; Hydrogen-Ion Concentration ; Kinetics ; Medical sciences ; Nitrophenols - chemistry ; Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions ; Pharmacology. Drug treatments ; Phenylbutazone - chemistry ; Phenylbutazone - pharmacology ; Rats ; Sarcosine - analogs & derivatives ; Sarcosine - chemistry ; Sheep ; Warfarin - chemistry</subject><ispartof>Biochemical pharmacology, 1992-09, Vol.44 (5), p.873-879</ispartof><rights>1992</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c452t-62d9ffcf83eca41f6fd076590cf182286858addafce6080c3976d761153053023</citedby><cites>FETCH-LOGICAL-c452t-62d9ffcf83eca41f6fd076590cf182286858addafce6080c3976d761153053023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-2952(92)90118-3$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5526766$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1382424$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Panjehshahin, Mohammad R.</creatorcontrib><creatorcontrib>Yates, Michael S.</creatorcontrib><creatorcontrib>Bowmer, Christopher J.</creatorcontrib><title>A comparison of drug binding sites on mammalian albumins</title><title>Biochemical pharmacology</title><addtitle>Biochem Pharmacol</addtitle><description>The fluorescent probes warfarin and dansylsarcosine are known to selectively interact with binding sites I and II, respectively, on human albumin. This paper investigates whether similar binding sites exist on bovine, dog, horse, sheep and rat albumins. Binding sites on albumins were studied by: (1) displacement of warfarin and dansylsarcosine by site I (phenylbutazone) and site II (diazepam) selective ligands; (2) the effects of non-esterified fatty acids (carbon chain lengths: C
5C-
20) and changes in pH (6–9) on the fluorescence of warfarin and dansylsarcosine; and (3) the ability of site selective ligands to inhibit hydrolysis of 4-nitrophenyl acetate. For bovine, dog, horse, human and sheep albumins the fluorescence of bound warfarin and dansylsarcosine was selectively decreased by phenylbutazone and diazepam, respectively. For these albumins medium chain fatty acids (C
7-C
12) reduced the fluorescence of dansylsarcosine (maximum inhibition with C
9) whereas long chain acids (C
12-C
20) enhanced the fluorescence of warfarin (maximum increases with C
12). In addition, changes in pH from 6 to 9 increased the fluorescence of warfarin and although site I ligands (warfarin/phenylbutazone) had no pronounced effects on 4-nitrophenyl acetate hydrolysis, site II ligands (dansylsareosine/diazepam) significantly inhibited this reaction. Rat albumin behaved differently from the other albumins studied in that the C
12-C
20 fatty acids and changes in pH did not enhance the fluorescence of warfarin. Moreover, the differential effects of site I and site II ligands on the fluorescence of warfarin/dansylsarcosine and hydrolysis of 4-nitrophenyl acetate were less apparent with rat albumin. The results suggest bovine, dog, horse and sheep albumins have binding sites for warfarin and dansylsarcosine with similar properties to sites I and II on human albumin. By contrast, the warfarin binding site and to a lesser degree the dansylsarcosine site, of rat albumin have different characteristics from these sites on the other albumins studied.</description><subject>Albumins - chemistry</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Binding, Competitive</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Dansyl Compounds - chemistry</subject><subject>Diazepam - chemistry</subject><subject>Diazepam - pharmacology</subject><subject>Dogs</subject><subject>Fatty Acids, Nonesterified - pharmacology</subject><subject>Fluorescence</subject><subject>General pharmacology</subject><subject>Horses</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Medical sciences</subject><subject>Nitrophenols - chemistry</subject><subject>Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions</subject><subject>Pharmacology. Drug treatments</subject><subject>Phenylbutazone - chemistry</subject><subject>Phenylbutazone - pharmacology</subject><subject>Rats</subject><subject>Sarcosine - analogs & derivatives</subject><subject>Sarcosine - chemistry</subject><subject>Sheep</subject><subject>Warfarin - chemistry</subject><issn>0006-2952</issn><issn>1873-2968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMtKxDAUhoMo4zj6BgpdiOiimkubJhthGLzBgBtdh0wuQ6RJx6QVfHtTOuhOOBCS_zuHkw-AcwRvEUT0DkJIS8xrfM3xDYcIsZIcgDliDcnPlB2C-S9yDE5S-hivjKIZmCHCcIWrOWDLQnV-J6NLXSg6W-g4bIuNC9qFbZFcb1KRAy-9l62ToZDtZvAupFNwZGWbzNn-XID3x4e31XO5fn16WS3Xpapq3JcUa26tsowYJStkqdWwoTWHyiKGMaOsZlJraZWhkEFFeEN1QxGqCcyFyQJcTXN3sfscTOqFd0mZtpXBdEMSDUGcQ8ozWE2gil1K0Vixi87L-C0QFKMwMX5fjDYEzzUKEyS3XeznDxtv9F_TZCjnl_tcJiVbG2VQLv1idY1pQ2nG7ifMZBdfzkSRlDNBGe2iUb3Qnft_jx8OWIUN</recordid><startdate>19920901</startdate><enddate>19920901</enddate><creator>Panjehshahin, Mohammad R.</creator><creator>Yates, Michael S.</creator><creator>Bowmer, Christopher J.</creator><general>Elsevier Inc</general><general>Elsevier Science</general><scope>IQODW</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>19920901</creationdate><title>A comparison of drug binding sites on mammalian albumins</title><author>Panjehshahin, Mohammad R. ; Yates, Michael S. ; Bowmer, Christopher J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c452t-62d9ffcf83eca41f6fd076590cf182286858addafce6080c3976d761153053023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Albumins - chemistry</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Binding, Competitive</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Dansyl Compounds - chemistry</topic><topic>Diazepam - chemistry</topic><topic>Diazepam - pharmacology</topic><topic>Dogs</topic><topic>Fatty Acids, Nonesterified - pharmacology</topic><topic>Fluorescence</topic><topic>General pharmacology</topic><topic>Horses</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Medical sciences</topic><topic>Nitrophenols - chemistry</topic><topic>Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions</topic><topic>Pharmacology. Drug treatments</topic><topic>Phenylbutazone - chemistry</topic><topic>Phenylbutazone - pharmacology</topic><topic>Rats</topic><topic>Sarcosine - analogs & derivatives</topic><topic>Sarcosine - chemistry</topic><topic>Sheep</topic><topic>Warfarin - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Panjehshahin, Mohammad R.</creatorcontrib><creatorcontrib>Yates, Michael S.</creatorcontrib><creatorcontrib>Bowmer, Christopher J.</creatorcontrib><collection>Pascal-Francis</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>Biochemical pharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Panjehshahin, Mohammad R.</au><au>Yates, Michael S.</au><au>Bowmer, Christopher J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A comparison of drug binding sites on mammalian albumins</atitle><jtitle>Biochemical pharmacology</jtitle><addtitle>Biochem Pharmacol</addtitle><date>1992-09-01</date><risdate>1992</risdate><volume>44</volume><issue>5</issue><spage>873</spage><epage>879</epage><pages>873-879</pages><issn>0006-2952</issn><eissn>1873-2968</eissn><coden>BCPCA6</coden><abstract>The fluorescent probes warfarin and dansylsarcosine are known to selectively interact with binding sites I and II, respectively, on human albumin. This paper investigates whether similar binding sites exist on bovine, dog, horse, sheep and rat albumins. Binding sites on albumins were studied by: (1) displacement of warfarin and dansylsarcosine by site I (phenylbutazone) and site II (diazepam) selective ligands; (2) the effects of non-esterified fatty acids (carbon chain lengths: C
5C-
20) and changes in pH (6–9) on the fluorescence of warfarin and dansylsarcosine; and (3) the ability of site selective ligands to inhibit hydrolysis of 4-nitrophenyl acetate. For bovine, dog, horse, human and sheep albumins the fluorescence of bound warfarin and dansylsarcosine was selectively decreased by phenylbutazone and diazepam, respectively. For these albumins medium chain fatty acids (C
7-C
12) reduced the fluorescence of dansylsarcosine (maximum inhibition with C
9) whereas long chain acids (C
12-C
20) enhanced the fluorescence of warfarin (maximum increases with C
12). In addition, changes in pH from 6 to 9 increased the fluorescence of warfarin and although site I ligands (warfarin/phenylbutazone) had no pronounced effects on 4-nitrophenyl acetate hydrolysis, site II ligands (dansylsareosine/diazepam) significantly inhibited this reaction. Rat albumin behaved differently from the other albumins studied in that the C
12-C
20 fatty acids and changes in pH did not enhance the fluorescence of warfarin. Moreover, the differential effects of site I and site II ligands on the fluorescence of warfarin/dansylsarcosine and hydrolysis of 4-nitrophenyl acetate were less apparent with rat albumin. The results suggest bovine, dog, horse and sheep albumins have binding sites for warfarin and dansylsarcosine with similar properties to sites I and II on human albumin. By contrast, the warfarin binding site and to a lesser degree the dansylsarcosine site, of rat albumin have different characteristics from these sites on the other albumins studied.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>1382424</pmid><doi>10.1016/0006-2952(92)90118-3</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-2952 |
| ispartof | Biochemical pharmacology, 1992-09, Vol.44 (5), p.873-879 |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_73199069 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Albumins - chemistry Animals Binding Sites Binding, Competitive Biological and medical sciences Cattle Dansyl Compounds - chemistry Diazepam - chemistry Diazepam - pharmacology Dogs Fatty Acids, Nonesterified - pharmacology Fluorescence General pharmacology Horses Humans Hydrogen-Ion Concentration Kinetics Medical sciences Nitrophenols - chemistry Pharmacokinetics. Pharmacogenetics. Drug-receptor interactions Pharmacology. Drug treatments Phenylbutazone - chemistry Phenylbutazone - pharmacology Rats Sarcosine - analogs & derivatives Sarcosine - chemistry Sheep Warfarin - chemistry |
| title | A comparison of drug binding sites on mammalian albumins |
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