Molecular weight of mitochondrial type B MAO in various organs of guinea pig
Molecular weights of mitochondrial type B monoamine oxidase (MAO) in guinea pig brain, liver and kidney were estimated, and their identities and multiplicity were studied. We ascertained what concentration of 3H-pargyline bound to type B MAO specifically from the inhibition curve toward serotonin (5...
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Veröffentlicht in: | Folia Pharmacologica Japonica 1985, Vol.85(1), pp.23-31 |
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description | Molecular weights of mitochondrial type B monoamine oxidase (MAO) in guinea pig brain, liver and kidney were estimated, and their identities and multiplicity were studied. We ascertained what concentration of 3H-pargyline bound to type B MAO specifically from the inhibition curve toward serotonin (5-HT) and β-phenylethylamine (β-PEA) by pargyline. Pargyline irreversibly binds to FAD in MAO at a one to one molecular ratio. 3H-pargyline bound to type B MAO specifically and irreversibly by incubation for 5 hr at 37°C, and SDS-disc electrophoresis was carried out using 3H-pargyline as a tracer. The molecular weight of MAO was estimated after specific binding of pargyline was corrected for non-specific binding. The molecular weight of type B MAO in every organ was found to be 60, 000, giving a single peak after solubilization with 6% SDS, but several peaks at higher molecular weight were found in each organ after solubilization with 2% SDS. In the brain, there appeared to be a peak of 100, 000, and it was suggested that the MAO existed as a dimer which was composed of a FAD containing subunit and a low molecular weight subunit containing no FAD. In the liver, there appeared to be peaks of 120, 000 and 240, 000, and it was suggested that the MAO existed as a dimer and tetramer. In the kidney, there appeared to be a peak of 180, 000, and MAO was suggested to exist as a trimer. |
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We ascertained what concentration of 3H-pargyline bound to type B MAO specifically from the inhibition curve toward serotonin (5-HT) and β-phenylethylamine (β-PEA) by pargyline. Pargyline irreversibly binds to FAD in MAO at a one to one molecular ratio. 3H-pargyline bound to type B MAO specifically and irreversibly by incubation for 5 hr at 37°C, and SDS-disc electrophoresis was carried out using 3H-pargyline as a tracer. The molecular weight of MAO was estimated after specific binding of pargyline was corrected for non-specific binding. The molecular weight of type B MAO in every organ was found to be 60, 000, giving a single peak after solubilization with 6% SDS, but several peaks at higher molecular weight were found in each organ after solubilization with 2% SDS. In the brain, there appeared to be a peak of 100, 000, and it was suggested that the MAO existed as a dimer which was composed of a FAD containing subunit and a low molecular weight subunit containing no FAD. In the liver, there appeared to be peaks of 120, 000 and 240, 000, and it was suggested that the MAO existed as a dimer and tetramer. In the kidney, there appeared to be a peak of 180, 000, and MAO was suggested to exist as a trimer.</description><identifier>ISSN: 0015-5691</identifier><identifier>EISSN: 1347-8397</identifier><identifier>DOI: 10.1254/fpj.85.23</identifier><identifier>PMID: 3988165</identifier><language>jpn</language><publisher>Japan: The Japanese Pharmacological Society</publisher><subject>amine oxidase (flavin-containing) ; Animals ; brain ; Brain - enzymology ; Chemical Phenomena ; Chemistry ; Electrophoresis, Disc ; Guinea Pigs ; Isoenzymes - isolation & purification ; kidney ; Kidney - enzymology ; liver ; Male ; mitochondria ; Mitochondria - enzymology ; Mitochondria, Liver - enzymology ; Molecular Weight ; Monoamine Oxidase - isolation & purification ; Organ Specificity ; pargyline</subject><ispartof>Folia Pharmacologica Japonica, 1985, Vol.85(1), pp.23-31</ispartof><rights>The Japanese PharmacologicalSociety</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,4010,27904,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3988165$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>OBATA, Toshio</creatorcontrib><creatorcontrib>HIRAI, Takafumi</creatorcontrib><creatorcontrib>KOBAYASHI, Shinichi</creatorcontrib><creatorcontrib>SHO, Sadayuki</creatorcontrib><creatorcontrib>YASUHARA, Hajime</creatorcontrib><title>Molecular weight of mitochondrial type B MAO in various organs of guinea pig</title><title>Folia Pharmacologica Japonica</title><addtitle>Nihon Yakurigaku Zasshi</addtitle><description>Molecular weights of mitochondrial type B monoamine oxidase (MAO) in guinea pig brain, liver and kidney were estimated, and their identities and multiplicity were studied. We ascertained what concentration of 3H-pargyline bound to type B MAO specifically from the inhibition curve toward serotonin (5-HT) and β-phenylethylamine (β-PEA) by pargyline. Pargyline irreversibly binds to FAD in MAO at a one to one molecular ratio. 3H-pargyline bound to type B MAO specifically and irreversibly by incubation for 5 hr at 37°C, and SDS-disc electrophoresis was carried out using 3H-pargyline as a tracer. The molecular weight of MAO was estimated after specific binding of pargyline was corrected for non-specific binding. The molecular weight of type B MAO in every organ was found to be 60, 000, giving a single peak after solubilization with 6% SDS, but several peaks at higher molecular weight were found in each organ after solubilization with 2% SDS. In the brain, there appeared to be a peak of 100, 000, and it was suggested that the MAO existed as a dimer which was composed of a FAD containing subunit and a low molecular weight subunit containing no FAD. In the liver, there appeared to be peaks of 120, 000 and 240, 000, and it was suggested that the MAO existed as a dimer and tetramer. In the kidney, there appeared to be a peak of 180, 000, and MAO was suggested to exist as a trimer.</description><subject>amine oxidase (flavin-containing)</subject><subject>Animals</subject><subject>brain</subject><subject>Brain - enzymology</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Electrophoresis, Disc</subject><subject>Guinea Pigs</subject><subject>Isoenzymes - isolation & purification</subject><subject>kidney</subject><subject>Kidney - enzymology</subject><subject>liver</subject><subject>Male</subject><subject>mitochondria</subject><subject>Mitochondria - enzymology</subject><subject>Mitochondria, Liver - enzymology</subject><subject>Molecular Weight</subject><subject>Monoamine Oxidase - isolation & purification</subject><subject>Organ Specificity</subject><subject>pargyline</subject><issn>0015-5691</issn><issn>1347-8397</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctOwzAQRS0EKlXpgg9A8opdil9J7GVb8ZJadQNry3HGqau8cBJQ_56gVt2ymbs4R6OrGYTuKVlQFosn1x4WMl4wfoWmlIs0klyl12hKCI2jOFH0Fs27zmeExClLE04naMKVlDSJp2izbUqwQ2kC_gFf7HvcOFz5vrH7ps6DNyXujy3gFd4ud9jX-NsE3wwdbkJh6u7PLgZfg8GtL-7QjTNlB_NzztDny_PH-i3a7F7f18tNdGBM9lEiLFHSMsJyRzOXUKVyBpBkjvE8NVmeKxAQqxxS4mwCjo-AWcEyaSwzjM_Q42lvG5qvAbpeV76zUJamhrGbThMiOeXkX5EKKgmXdBQfzuKQVZDrNvjKhKM-32nkqxM_dL0p4MJN6L0tQY8_oEoILWNNT4PxC7R7EzTU_Bd1EIGo</recordid><startdate>1985</startdate><enddate>1985</enddate><creator>OBATA, Toshio</creator><creator>HIRAI, Takafumi</creator><creator>KOBAYASHI, Shinichi</creator><creator>SHO, Sadayuki</creator><creator>YASUHARA, Hajime</creator><general>The Japanese Pharmacological Society</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>1985</creationdate><title>Molecular weight of mitochondrial type B MAO in various organs of guinea pig</title><author>OBATA, Toshio ; HIRAI, Takafumi ; KOBAYASHI, Shinichi ; SHO, Sadayuki ; YASUHARA, Hajime</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j228t-64c098c202df1bf6199d2ee6bf23d7abdd9e4e59de70fc6ef3f232c42b8ac2a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>jpn</language><creationdate>1985</creationdate><topic>amine oxidase (flavin-containing)</topic><topic>Animals</topic><topic>brain</topic><topic>Brain - enzymology</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Electrophoresis, Disc</topic><topic>Guinea Pigs</topic><topic>Isoenzymes - isolation & purification</topic><topic>kidney</topic><topic>Kidney - enzymology</topic><topic>liver</topic><topic>Male</topic><topic>mitochondria</topic><topic>Mitochondria - enzymology</topic><topic>Mitochondria, Liver - enzymology</topic><topic>Molecular Weight</topic><topic>Monoamine Oxidase - isolation & purification</topic><topic>Organ Specificity</topic><topic>pargyline</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>OBATA, Toshio</creatorcontrib><creatorcontrib>HIRAI, Takafumi</creatorcontrib><creatorcontrib>KOBAYASHI, Shinichi</creatorcontrib><creatorcontrib>SHO, Sadayuki</creatorcontrib><creatorcontrib>YASUHARA, Hajime</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>Folia Pharmacologica Japonica</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>OBATA, Toshio</au><au>HIRAI, Takafumi</au><au>KOBAYASHI, Shinichi</au><au>SHO, Sadayuki</au><au>YASUHARA, Hajime</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular weight of mitochondrial type B MAO in various organs of guinea pig</atitle><jtitle>Folia Pharmacologica Japonica</jtitle><addtitle>Nihon Yakurigaku Zasshi</addtitle><date>1985</date><risdate>1985</risdate><volume>85</volume><issue>1</issue><spage>23</spage><epage>31</epage><pages>23-31</pages><issn>0015-5691</issn><eissn>1347-8397</eissn><abstract>Molecular weights of mitochondrial type B monoamine oxidase (MAO) in guinea pig brain, liver and kidney were estimated, and their identities and multiplicity were studied. We ascertained what concentration of 3H-pargyline bound to type B MAO specifically from the inhibition curve toward serotonin (5-HT) and β-phenylethylamine (β-PEA) by pargyline. Pargyline irreversibly binds to FAD in MAO at a one to one molecular ratio. 3H-pargyline bound to type B MAO specifically and irreversibly by incubation for 5 hr at 37°C, and SDS-disc electrophoresis was carried out using 3H-pargyline as a tracer. The molecular weight of MAO was estimated after specific binding of pargyline was corrected for non-specific binding. The molecular weight of type B MAO in every organ was found to be 60, 000, giving a single peak after solubilization with 6% SDS, but several peaks at higher molecular weight were found in each organ after solubilization with 2% SDS. In the brain, there appeared to be a peak of 100, 000, and it was suggested that the MAO existed as a dimer which was composed of a FAD containing subunit and a low molecular weight subunit containing no FAD. In the liver, there appeared to be peaks of 120, 000 and 240, 000, and it was suggested that the MAO existed as a dimer and tetramer. In the kidney, there appeared to be a peak of 180, 000, and MAO was suggested to exist as a trimer.</abstract><cop>Japan</cop><pub>The Japanese Pharmacological Society</pub><pmid>3988165</pmid><doi>10.1254/fpj.85.23</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | amine oxidase (flavin-containing) Animals brain Brain - enzymology Chemical Phenomena Chemistry Electrophoresis, Disc Guinea Pigs Isoenzymes - isolation & purification kidney Kidney - enzymology liver Male mitochondria Mitochondria - enzymology Mitochondria, Liver - enzymology Molecular Weight Monoamine Oxidase - isolation & purification Organ Specificity pargyline |
title | Molecular weight of mitochondrial type B MAO in various organs of guinea pig |
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