Liver cytosolic aldehyde dehydrogenases in rats with different predisposition to induction by phenobarbital: Partial purification and characterization of the enzymes at basal state
1. 1. Liver cytosolic aldehyde dehydrogenases were partially purified from rats with different genetic predisposition to induction of aldehyde dehydrogenase activity by phenobarbital. The enzymes were studied at basal state without any pretreatment with an inducer. 2. 2. The main aldehyde dehydrogen...
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| Veröffentlicht in: | International journal of biochemistry 1984, Vol.16 (6), p.659-666 |
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| container_title | International journal of biochemistry |
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| creator | Törrönen, Riitta Laaksonen, Mariitta |
| description | 1.
1. Liver cytosolic aldehyde dehydrogenases were partially purified from rats with different genetic predisposition to induction of aldehyde dehydrogenase activity by phenobarbital. The enzymes were studied at basal state without any pretreatment with an inducer.
2.
2. The main aldehyde dehydrogenases from the non-, high- and intermediate reactor animals could not be differentiated by substrate specificity or thermostability.
3.
3. The enzyme from the non-reactor rats was more resistant to changes of pH and to the inhibitory effects of disulfiram than the enzymes from the high- or intermediate reactors.
4.
4. Immunochemical studies suggested a dissimilarity of these enzymes. |
| doi_str_mv | 10.1016/0020-711X(84)90035-1 |
| format | Article |
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1. Liver cytosolic aldehyde dehydrogenases were partially purified from rats with different genetic predisposition to induction of aldehyde dehydrogenase activity by phenobarbital. The enzymes were studied at basal state without any pretreatment with an inducer.
2.
2. The main aldehyde dehydrogenases from the non-, high- and intermediate reactor animals could not be differentiated by substrate specificity or thermostability.
3.
3. The enzyme from the non-reactor rats was more resistant to changes of pH and to the inhibitory effects of disulfiram than the enzymes from the high- or intermediate reactors.
4.
4. Immunochemical studies suggested a dissimilarity of these enzymes.</description><identifier>ISSN: 0020-711X</identifier><identifier>DOI: 10.1016/0020-711X(84)90035-1</identifier><identifier>PMID: 6468731</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Aldehyde Dehydrogenase ; Aldehyde Oxidoreductases - biosynthesis ; Aldehyde Oxidoreductases - isolation & purification ; Animals ; cytosol ; Cytosol - enzymology ; Disulfiram - pharmacology ; Enzyme Induction ; Female ; Hydrogen-Ion Concentration ; Isoenzymes - biosynthesis ; Isoenzymes - isolation & purification ; Kinetics ; liver ; Liver - enzymology ; Phenobarbital - pharmacology ; Rats ; Rats, Inbred Strains ; Substrate Specificity</subject><ispartof>International journal of biochemistry, 1984, Vol.16 (6), p.659-666</ispartof><rights>1984</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6468731$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Törrönen, Riitta</creatorcontrib><creatorcontrib>Laaksonen, Mariitta</creatorcontrib><title>Liver cytosolic aldehyde dehydrogenases in rats with different predisposition to induction by phenobarbital: Partial purification and characterization of the enzymes at basal state</title><title>International journal of biochemistry</title><addtitle>Int J Biochem</addtitle><description>1.
1. Liver cytosolic aldehyde dehydrogenases were partially purified from rats with different genetic predisposition to induction of aldehyde dehydrogenase activity by phenobarbital. The enzymes were studied at basal state without any pretreatment with an inducer.
2.
2. The main aldehyde dehydrogenases from the non-, high- and intermediate reactor animals could not be differentiated by substrate specificity or thermostability.
3.
3. The enzyme from the non-reactor rats was more resistant to changes of pH and to the inhibitory effects of disulfiram than the enzymes from the high- or intermediate reactors.
4.
4. Immunochemical studies suggested a dissimilarity of these enzymes.</description><subject>Aldehyde Dehydrogenase</subject><subject>Aldehyde Oxidoreductases - biosynthesis</subject><subject>Aldehyde Oxidoreductases - isolation & purification</subject><subject>Animals</subject><subject>cytosol</subject><subject>Cytosol - enzymology</subject><subject>Disulfiram - pharmacology</subject><subject>Enzyme Induction</subject><subject>Female</subject><subject>Hydrogen-Ion Concentration</subject><subject>Isoenzymes - biosynthesis</subject><subject>Isoenzymes - isolation & purification</subject><subject>Kinetics</subject><subject>liver</subject><subject>Liver - enzymology</subject><subject>Phenobarbital - pharmacology</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Substrate Specificity</subject><issn>0020-711X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2L1jAQgHtQ1nX1HyjkJHqoJmnSph4EWdxVeEEPCt7CNJnaSN-kJulK93f5A837gVdPw8w8yTDzVNUzRl8zyto3lHJad4x9f6nEq57SRtbsQXX5r_yoepzST0pZrwS7qC5a0aquYZfVn527w0jMlkMKszMEZovTZpEcQww_0EPCRJwnEXIiv12eiHXjiBF9JktE69ISkssueJJDAe1qjsmwkWVCHwaIg8swvyVfIGYHM1nW6EZn4IiBt8RMEMFkjO7-VAwjyRMS9PfbvkyHTAZI5WXKkPFJ9XCEOeHTc7yqvt18-Hr9sd59vv10_X5XI-95rnvElncNtAokNkpJLoZeAreSSspFM3DoWymb3oKkgknEoSugoBa5EnxsrqoXp3-XGH6tmLLeu2RwnsFjWJNWjFPRcf5fkDU9bUQnCvj8DK7DHq1eottD3PTZR-m_O_WxrHXnMOpkHHpTjhzRZG2D04zqg3N9kKsPcrUS-ui8zPkL_eykDA</recordid><startdate>1984</startdate><enddate>1984</enddate><creator>Törrönen, Riitta</creator><creator>Laaksonen, Mariitta</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>1984</creationdate><title>Liver cytosolic aldehyde dehydrogenases in rats with different predisposition to induction by phenobarbital: Partial purification and characterization of the enzymes at basal state</title><author>Törrönen, Riitta ; Laaksonen, Mariitta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e292t-9ee6273a68a5e388524b95a2d5050243b2a965539da50415eeb75e340de2842f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>Aldehyde Dehydrogenase</topic><topic>Aldehyde Oxidoreductases - biosynthesis</topic><topic>Aldehyde Oxidoreductases - isolation & purification</topic><topic>Animals</topic><topic>cytosol</topic><topic>Cytosol - enzymology</topic><topic>Disulfiram - pharmacology</topic><topic>Enzyme Induction</topic><topic>Female</topic><topic>Hydrogen-Ion Concentration</topic><topic>Isoenzymes - biosynthesis</topic><topic>Isoenzymes - isolation & purification</topic><topic>Kinetics</topic><topic>liver</topic><topic>Liver - enzymology</topic><topic>Phenobarbital - pharmacology</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Substrate Specificity</topic><toplevel>online_resources</toplevel><creatorcontrib>Törrönen, Riitta</creatorcontrib><creatorcontrib>Laaksonen, Mariitta</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Törrönen, Riitta</au><au>Laaksonen, Mariitta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Liver cytosolic aldehyde dehydrogenases in rats with different predisposition to induction by phenobarbital: Partial purification and characterization of the enzymes at basal state</atitle><jtitle>International journal of biochemistry</jtitle><addtitle>Int J Biochem</addtitle><date>1984</date><risdate>1984</risdate><volume>16</volume><issue>6</issue><spage>659</spage><epage>666</epage><pages>659-666</pages><issn>0020-711X</issn><abstract>1.
1. Liver cytosolic aldehyde dehydrogenases were partially purified from rats with different genetic predisposition to induction of aldehyde dehydrogenase activity by phenobarbital. The enzymes were studied at basal state without any pretreatment with an inducer.
2.
2. The main aldehyde dehydrogenases from the non-, high- and intermediate reactor animals could not be differentiated by substrate specificity or thermostability.
3.
3. The enzyme from the non-reactor rats was more resistant to changes of pH and to the inhibitory effects of disulfiram than the enzymes from the high- or intermediate reactors.
4.
4. Immunochemical studies suggested a dissimilarity of these enzymes.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>6468731</pmid><doi>10.1016/0020-711X(84)90035-1</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0020-711X |
| ispartof | International journal of biochemistry, 1984, Vol.16 (6), p.659-666 |
| issn | 0020-711X |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Aldehyde Dehydrogenase Aldehyde Oxidoreductases - biosynthesis Aldehyde Oxidoreductases - isolation & purification Animals cytosol Cytosol - enzymology Disulfiram - pharmacology Enzyme Induction Female Hydrogen-Ion Concentration Isoenzymes - biosynthesis Isoenzymes - isolation & purification Kinetics liver Liver - enzymology Phenobarbital - pharmacology Rats Rats, Inbred Strains Substrate Specificity |
| title | Liver cytosolic aldehyde dehydrogenases in rats with different predisposition to induction by phenobarbital: Partial purification and characterization of the enzymes at basal state |
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