Purification and properties of pig liver esterase
A homogenous preparation of pig liver aliesterase (EC 3.1.1.1) was obtained by the use of preparative starch-gel electrophoresis. The esterolytic activity of this preparation is markedly accelerated at high substrate concentration. Two active sites on the molecule may account for this unusual kineti...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1969-01, Vol.135 (1), p.259-264 |
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| container_title | Archives of biochemistry and biophysics |
| container_volume | 135 |
| creator | Levy, Milton Ocken, Paul R. |
| description | A homogenous preparation of pig liver aliesterase (EC 3.1.1.1) was obtained by the use of preparative starch-gel electrophoresis. The esterolytic activity of this preparation is markedly accelerated at high substrate concentration. Two active sites on the molecule may account for this unusual kinetic behavior. The sites may be identical as in a monomer-dimer equilibrium or they may be nonidentical and different in function. The esterase apparently is neither stereospecific nor stereoselective, and it did not exhibit an asymmetric active site. The enzyme hydrolyzes esters that are nonionic at a much greater rate than charged analogs. Half-esters of dicarboxylic acids are neither substrates nor inhibitors. Apparently an anionic charge on an ester inhibits the association between the esterase and ester. |
| doi_str_mv | 10.1016/0003-9861(69)90538-4 |
| format | Article |
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The esterolytic activity of this preparation is markedly accelerated at high substrate concentration. Two active sites on the molecule may account for this unusual kinetic behavior. The sites may be identical as in a monomer-dimer equilibrium or they may be nonidentical and different in function. The esterase apparently is neither stereospecific nor stereoselective, and it did not exhibit an asymmetric active site. The enzyme hydrolyzes esters that are nonionic at a much greater rate than charged analogs. Half-esters of dicarboxylic acids are neither substrates nor inhibitors. Apparently an anionic charge on an ester inhibits the association between the esterase and ester.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(69)90538-4</identifier><identifier>PMID: 5362929</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetone ; Ammonia ; Animals ; Binding Sites ; Chromatography, DEAE-Cellulose ; Dicarboxylic Acids ; Electrophoresis ; Esterases - antagonists & inhibitors ; Esterases - isolation & purification ; Gels ; Kinetics ; Liver - enzymology ; Methods ; Quaternary Ammonium Compounds ; Starch ; Swine</subject><ispartof>Archives of biochemistry and biophysics, 1969-01, Vol.135 (1), p.259-264</ispartof><rights>1969</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-67ff01e9aec67603074145c6dacab61269a9685d697011f924b10d4d51f8744e3</citedby><cites>FETCH-LOGICAL-c423t-67ff01e9aec67603074145c6dacab61269a9685d697011f924b10d4d51f8744e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986169905384$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5362929$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Levy, Milton</creatorcontrib><creatorcontrib>Ocken, Paul R.</creatorcontrib><title>Purification and properties of pig liver esterase</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>A homogenous preparation of pig liver aliesterase (EC 3.1.1.1) was obtained by the use of preparative starch-gel electrophoresis. The esterolytic activity of this preparation is markedly accelerated at high substrate concentration. Two active sites on the molecule may account for this unusual kinetic behavior. The sites may be identical as in a monomer-dimer equilibrium or they may be nonidentical and different in function. The esterase apparently is neither stereospecific nor stereoselective, and it did not exhibit an asymmetric active site. The enzyme hydrolyzes esters that are nonionic at a much greater rate than charged analogs. Half-esters of dicarboxylic acids are neither substrates nor inhibitors. Apparently an anionic charge on an ester inhibits the association between the esterase and ester.</description><subject>Acetone</subject><subject>Ammonia</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Dicarboxylic Acids</subject><subject>Electrophoresis</subject><subject>Esterases - antagonists & inhibitors</subject><subject>Esterases - isolation & purification</subject><subject>Gels</subject><subject>Kinetics</subject><subject>Liver - enzymology</subject><subject>Methods</subject><subject>Quaternary Ammonium Compounds</subject><subject>Starch</subject><subject>Swine</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1969</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1OwzAQhC0EKqXwBiDlhOAQsGNnE1-QUMWfVAkOcLZce42M0iTYSSXeHpdWPXLaw8zO7H6EnDN6wyiDW0opz2UN7ArktaQlr3NxQKaMSsgpr8Uhme4tx-Qkxi9KGRNQTMik5FDIQk4JexuDd97owXdtplub9aHrMQweY9a5rPefWePXGDKMAwYd8ZQcOd1EPNvNGfl4fHifP-eL16eX-f0iN6LgQw6Vc5Sh1GigAsppJZgoDVht9BJYAVJLqEsLskpXOVmIJaNW2JK5uhIC-YxcbnPTQd9jalcrHw02jW6xG6OqBS-5ZJCMYms0oYsxoFN98CsdfhSjakNKbTCoDQYFUv2RUiKtXezyx-UK7X5phybpd1sd05Nrj0FF47E1aH1AMyjb-f8LfgHL9HYU</recordid><startdate>19690101</startdate><enddate>19690101</enddate><creator>Levy, Milton</creator><creator>Ocken, Paul R.</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>19690101</creationdate><title>Purification and properties of pig liver esterase</title><author>Levy, Milton ; Ocken, Paul R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-67ff01e9aec67603074145c6dacab61269a9685d697011f924b10d4d51f8744e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1969</creationdate><topic>Acetone</topic><topic>Ammonia</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Dicarboxylic Acids</topic><topic>Electrophoresis</topic><topic>Esterases - antagonists & inhibitors</topic><topic>Esterases - isolation & purification</topic><topic>Gels</topic><topic>Kinetics</topic><topic>Liver - enzymology</topic><topic>Methods</topic><topic>Quaternary Ammonium Compounds</topic><topic>Starch</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Levy, Milton</creatorcontrib><creatorcontrib>Ocken, Paul R.</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>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Levy, Milton</au><au>Ocken, Paul R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and properties of pig liver esterase</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1969-01-01</date><risdate>1969</risdate><volume>135</volume><issue>1</issue><spage>259</spage><epage>264</epage><pages>259-264</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>A homogenous preparation of pig liver aliesterase (EC 3.1.1.1) was obtained by the use of preparative starch-gel electrophoresis. The esterolytic activity of this preparation is markedly accelerated at high substrate concentration. Two active sites on the molecule may account for this unusual kinetic behavior. The sites may be identical as in a monomer-dimer equilibrium or they may be nonidentical and different in function. The esterase apparently is neither stereospecific nor stereoselective, and it did not exhibit an asymmetric active site. The enzyme hydrolyzes esters that are nonionic at a much greater rate than charged analogs. Half-esters of dicarboxylic acids are neither substrates nor inhibitors. Apparently an anionic charge on an ester inhibits the association between the esterase and ester.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>5362929</pmid><doi>10.1016/0003-9861(69)90538-4</doi><tpages>6</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1969-01, Vol.135 (1), p.259-264 |
| issn | 0003-9861 1096-0384 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Acetone Ammonia Animals Binding Sites Chromatography, DEAE-Cellulose Dicarboxylic Acids Electrophoresis Esterases - antagonists & inhibitors Esterases - isolation & purification Gels Kinetics Liver - enzymology Methods Quaternary Ammonium Compounds Starch Swine |
| title | Purification and properties of pig liver esterase |
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