Heterogeneity of NADPH‐Dependent Aldehyde Reductase from Human and Rat Brain
1 Four multiple molecular forms of NADPH‐dependent aldehyde reductase are isolated by ion‐exchange and gel chromatography from human brain. Using the same procedure two multiple forms of NADPH‐dependent aldehyde reductase are found in rat brain. 2 The molecular weight of two of the forms of human br...
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| Veröffentlicht in: | European journal of biochemistry 1973-08, Vol.37 (1), p.69-77 |
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| container_title | European journal of biochemistry |
| container_volume | 37 |
| creator | Ris, Margret M. Wartburg, Jean‐Pierre |
| description | 1
Four multiple molecular forms of NADPH‐dependent aldehyde reductase are isolated by ion‐exchange and gel chromatography from human brain. Using the same procedure two multiple forms of NADPH‐dependent aldehyde reductase are found in rat brain.
2
The molecular weight of two of the forms of human brain aldehyde reductase is 40000 and of the other two forms it is 44000.
3
Large differences with respect to substrate specificity with a wide range of aliphatic and aromatic aldehydes are observed between the multiple enzyme forms of each species.
4
All enzyme forms use NADPH as coenzyme; additionally one enzyme of each species can use NADH as well.
5
Classical inhibitors of aldehyde and alcohol dehydrogenase do not affect the activity of the multiple molecular forms of aldehyde reductase from human and rat brain, but psychoactive substances such as barbiturates and chlorpromazine as well as “biogenic” acids are inhibitory. |
| doi_str_mv | 10.1111/j.1432-1033.1973.tb02958.x |
| format | Article |
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Four multiple molecular forms of NADPH‐dependent aldehyde reductase are isolated by ion‐exchange and gel chromatography from human brain. Using the same procedure two multiple forms of NADPH‐dependent aldehyde reductase are found in rat brain.
2
The molecular weight of two of the forms of human brain aldehyde reductase is 40000 and of the other two forms it is 44000.
3
Large differences with respect to substrate specificity with a wide range of aliphatic and aromatic aldehydes are observed between the multiple enzyme forms of each species.
4
All enzyme forms use NADPH as coenzyme; additionally one enzyme of each species can use NADH as well.
5
Classical inhibitors of aldehyde and alcohol dehydrogenase do not affect the activity of the multiple molecular forms of aldehyde reductase from human and rat brain, but psychoactive substances such as barbiturates and chlorpromazine as well as “biogenic” acids are inhibitory.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1973.tb02958.x</identifier><identifier>PMID: 4147090</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Aldehyde Oxidoreductases - analysis ; Aldehyde Oxidoreductases - antagonists & inhibitors ; Aldehydes ; Animals ; Barbiturates ; Brain - enzymology ; Cell Fractionation ; Chlorpromazine ; Chromatography, DEAE-Cellulose ; Chromatography, Gel ; Chromatography, Ion Exchange ; Female ; Humans ; Isoenzymes ; Kinetics ; Male ; Molecular Weight ; NAD ; NADP ; Rats ; Structure-Activity Relationship</subject><ispartof>European journal of biochemistry, 1973-08, Vol.37 (1), p.69-77</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3989-e96c1ae24decb4161aa8fb1a51776551eaa2ca2aec3e489ad4d5f306a630339d3</citedby><cites>FETCH-LOGICAL-c3989-e96c1ae24decb4161aa8fb1a51776551eaa2ca2aec3e489ad4d5f306a630339d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4147090$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ris, Margret M.</creatorcontrib><creatorcontrib>Wartburg, Jean‐Pierre</creatorcontrib><title>Heterogeneity of NADPH‐Dependent Aldehyde Reductase from Human and Rat Brain</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>1
Four multiple molecular forms of NADPH‐dependent aldehyde reductase are isolated by ion‐exchange and gel chromatography from human brain. Using the same procedure two multiple forms of NADPH‐dependent aldehyde reductase are found in rat brain.
2
The molecular weight of two of the forms of human brain aldehyde reductase is 40000 and of the other two forms it is 44000.
3
Large differences with respect to substrate specificity with a wide range of aliphatic and aromatic aldehydes are observed between the multiple enzyme forms of each species.
4
All enzyme forms use NADPH as coenzyme; additionally one enzyme of each species can use NADH as well.
5
Classical inhibitors of aldehyde and alcohol dehydrogenase do not affect the activity of the multiple molecular forms of aldehyde reductase from human and rat brain, but psychoactive substances such as barbiturates and chlorpromazine as well as “biogenic” acids are inhibitory.</description><subject>Aldehyde Oxidoreductases - analysis</subject><subject>Aldehyde Oxidoreductases - antagonists & inhibitors</subject><subject>Aldehydes</subject><subject>Animals</subject><subject>Barbiturates</subject><subject>Brain - enzymology</subject><subject>Cell Fractionation</subject><subject>Chlorpromazine</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Female</subject><subject>Humans</subject><subject>Isoenzymes</subject><subject>Kinetics</subject><subject>Male</subject><subject>Molecular Weight</subject><subject>NAD</subject><subject>NADP</subject><subject>Rats</subject><subject>Structure-Activity Relationship</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkMlOwzAQhi0EKmV5BCSLA7cEO3acmANSF6BIFaACZ2saTyBVlhInor3xCDwjT0KqVtyZyxz-ZTQfIeec-byby4XPpQg8zoTwuY6E38xZoMPYX-2R_p-0T_qMcel1ijokR84tGGNKq6hHepLLiGnWJw8TbLCu3rDErFnTKqUPg_HT5Ofre4xLLC2WDR3kFt_XFukMbZs04JCmdVXQSVtASaG0dAYNHdaQlSfkIIXc4eluH5PX25uX0cSbPt7djwZTLxE61h5qlXDAQFpM5pIrDhCncw4hjyIVhhwBggQCwESgjDVYacNUMAVKdI9pK47JxbZ3WVcfLbrGFJlLMM-hxKp1Jg5YEEsZdcarrTGpK-dqTM2yzgqo14Yzs4FpFmZDzGyImQ1Ms4NpVl34bHelnRdo_6I7ep1-vdU_sxzX_2g2tzfDZ6XFL9YOhNs</recordid><startdate>197308</startdate><enddate>197308</enddate><creator>Ris, Margret M.</creator><creator>Wartburg, Jean‐Pierre</creator><general>Blackwell Publishing Ltd</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>197308</creationdate><title>Heterogeneity of NADPH‐Dependent Aldehyde Reductase from Human and Rat Brain</title><author>Ris, Margret M. ; Wartburg, Jean‐Pierre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3989-e96c1ae24decb4161aa8fb1a51776551eaa2ca2aec3e489ad4d5f306a630339d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Aldehyde Oxidoreductases - analysis</topic><topic>Aldehyde Oxidoreductases - antagonists & inhibitors</topic><topic>Aldehydes</topic><topic>Animals</topic><topic>Barbiturates</topic><topic>Brain - enzymology</topic><topic>Cell Fractionation</topic><topic>Chlorpromazine</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>Female</topic><topic>Humans</topic><topic>Isoenzymes</topic><topic>Kinetics</topic><topic>Male</topic><topic>Molecular Weight</topic><topic>NAD</topic><topic>NADP</topic><topic>Rats</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ris, Margret M.</creatorcontrib><creatorcontrib>Wartburg, Jean‐Pierre</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>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ris, Margret M.</au><au>Wartburg, Jean‐Pierre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heterogeneity of NADPH‐Dependent Aldehyde Reductase from Human and Rat Brain</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1973-08</date><risdate>1973</risdate><volume>37</volume><issue>1</issue><spage>69</spage><epage>77</epage><pages>69-77</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>1
Four multiple molecular forms of NADPH‐dependent aldehyde reductase are isolated by ion‐exchange and gel chromatography from human brain. Using the same procedure two multiple forms of NADPH‐dependent aldehyde reductase are found in rat brain.
2
The molecular weight of two of the forms of human brain aldehyde reductase is 40000 and of the other two forms it is 44000.
3
Large differences with respect to substrate specificity with a wide range of aliphatic and aromatic aldehydes are observed between the multiple enzyme forms of each species.
4
All enzyme forms use NADPH as coenzyme; additionally one enzyme of each species can use NADH as well.
5
Classical inhibitors of aldehyde and alcohol dehydrogenase do not affect the activity of the multiple molecular forms of aldehyde reductase from human and rat brain, but psychoactive substances such as barbiturates and chlorpromazine as well as “biogenic” acids are inhibitory.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>4147090</pmid><doi>10.1111/j.1432-1033.1973.tb02958.x</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1973-08, Vol.37 (1), p.69-77 |
| issn | 0014-2956 1432-1033 |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Aldehyde Oxidoreductases - analysis Aldehyde Oxidoreductases - antagonists & inhibitors Aldehydes Animals Barbiturates Brain - enzymology Cell Fractionation Chlorpromazine Chromatography, DEAE-Cellulose Chromatography, Gel Chromatography, Ion Exchange Female Humans Isoenzymes Kinetics Male Molecular Weight NAD NADP Rats Structure-Activity Relationship |
| title | Heterogeneity of NADPH‐Dependent Aldehyde Reductase from Human and Rat Brain |
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