Characterization of Cationic Acid Phosphatase Isozyme from Rat Liver Mitochondria
Acid phosphatase isozyme was highly purified from rat liver mitochondrial fraction. The enzyme showed an isoelectric point value of above 9.5 on isoelectric focusing, and the apparent molecular weight was estimated to be 32000 by Sephadex G-100 gel filtration or 16000 by sodium dodecyl sulfate-polya...
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| Veröffentlicht in: | Chemical & pharmaceutical bulletin 1992/05/25, Vol.40(5), pp.1231-1235 |
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| container_title | Chemical & pharmaceutical bulletin |
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| creator | FUJIMOTO, Sadaki MURAKAMI, Kazuki HOSODA, Takashi YAMAMOTO, Yuusuke WATANABE, Katsuichi MORINAKA, Yoshinori OHARA, Akira |
| description | Acid phosphatase isozyme was highly purified from rat liver mitochondrial fraction. The enzyme showed an isoelectric point value of above 9.5 on isoelectric focusing, and the apparent molecular weight was estimated to be 32000 by Sephadex G-100 gel filtration or 16000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme catalyzed the hydrolysis of adenosine 5'-triphosphate, adenosine 5'-diphosphate, thiamine pyrophosphate, inorganic pyrophosphate, and phosphoproteion such as casein and phosvitin, but not of several phosphomonoesters, except for p-nitrophenyl phosphate and o-phosphotyrosine. The enzyme was not inhibited by L-(+)-tartrate, and was significantly activated by Fe2+ and reducing agents such as ascorbic acid, L-cysteine, and dithiothreitol. The enzyme was found to be distributed in various rat tissues including liver, spleen, kidney, small intestine, lung, stomach, brain and beart, but not in skeletal muscle. |
| doi_str_mv | 10.1248/cpb.40.1231 |
| format | Article |
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The enzyme showed an isoelectric point value of above 9.5 on isoelectric focusing, and the apparent molecular weight was estimated to be 32000 by Sephadex G-100 gel filtration or 16000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme catalyzed the hydrolysis of adenosine 5'-triphosphate, adenosine 5'-diphosphate, thiamine pyrophosphate, inorganic pyrophosphate, and phosphoproteion such as casein and phosvitin, but not of several phosphomonoesters, except for p-nitrophenyl phosphate and o-phosphotyrosine. The enzyme was not inhibited by L-(+)-tartrate, and was significantly activated by Fe2+ and reducing agents such as ascorbic acid, L-cysteine, and dithiothreitol. The enzyme was found to be distributed in various rat tissues including liver, spleen, kidney, small intestine, lung, stomach, brain and beart, but not in skeletal muscle.</description><identifier>ISSN: 0009-2363</identifier><identifier>EISSN: 1347-5223</identifier><identifier>DOI: 10.1248/cpb.40.1231</identifier><identifier>PMID: 1394639</identifier><language>eng</language><publisher>Japan: The Pharmaceutical Society of Japan</publisher><subject>acid phosphatase ; Acid Phosphatase - antagonists & inhibitors ; Acid Phosphatase - chemistry ; Acid Phosphatase - metabolism ; Animals ; Cations ; Enzyme Activation ; Isoelectric Point ; Isoenzymes - antagonists & inhibitors ; Isoenzymes - chemistry ; Isoenzymes - metabolism ; Male ; mitochondria ; Mitochondria, Liver - enzymology ; Molecular Weight ; protein phosphatase ; rat liver ; Rats ; Rats, Wistar ; Substrate Specificity</subject><ispartof>Chemical and Pharmaceutical Bulletin, 1992/05/25, Vol.40(5), pp.1231-1235</ispartof><rights>The Pharmaceutical Society of Japan</rights><rights>Copyright Japan Science and Technology Agency 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1881,4014,27914,27915,27916</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1394639$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>FUJIMOTO, Sadaki</creatorcontrib><creatorcontrib>MURAKAMI, Kazuki</creatorcontrib><creatorcontrib>HOSODA, Takashi</creatorcontrib><creatorcontrib>YAMAMOTO, Yuusuke</creatorcontrib><creatorcontrib>WATANABE, Katsuichi</creatorcontrib><creatorcontrib>MORINAKA, Yoshinori</creatorcontrib><creatorcontrib>OHARA, Akira</creatorcontrib><title>Characterization of Cationic Acid Phosphatase Isozyme from Rat Liver Mitochondria</title><title>Chemical & pharmaceutical bulletin</title><addtitle>Chem. Pharm. Bull.</addtitle><description>Acid phosphatase isozyme was highly purified from rat liver mitochondrial fraction. The enzyme showed an isoelectric point value of above 9.5 on isoelectric focusing, and the apparent molecular weight was estimated to be 32000 by Sephadex G-100 gel filtration or 16000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme catalyzed the hydrolysis of adenosine 5'-triphosphate, adenosine 5'-diphosphate, thiamine pyrophosphate, inorganic pyrophosphate, and phosphoproteion such as casein and phosvitin, but not of several phosphomonoesters, except for p-nitrophenyl phosphate and o-phosphotyrosine. The enzyme was not inhibited by L-(+)-tartrate, and was significantly activated by Fe2+ and reducing agents such as ascorbic acid, L-cysteine, and dithiothreitol. The enzyme was found to be distributed in various rat tissues including liver, spleen, kidney, small intestine, lung, stomach, brain and beart, but not in skeletal muscle.</description><subject>acid phosphatase</subject><subject>Acid Phosphatase - antagonists & inhibitors</subject><subject>Acid Phosphatase - chemistry</subject><subject>Acid Phosphatase - metabolism</subject><subject>Animals</subject><subject>Cations</subject><subject>Enzyme Activation</subject><subject>Isoelectric Point</subject><subject>Isoenzymes - antagonists & inhibitors</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - metabolism</subject><subject>Male</subject><subject>mitochondria</subject><subject>Mitochondria, Liver - enzymology</subject><subject>Molecular Weight</subject><subject>protein phosphatase</subject><subject>rat liver</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Substrate Specificity</subject><issn>0009-2363</issn><issn>1347-5223</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUlLAzEAhYMotS4nz0JA8CKjWWc5Sl2h4oKeQ5LJ2JTOpCapYH-9GUcseEkeeR-PxwsARxidY8LKC71U56zXFG-BMaasyDghdBuMEUJVRmhOd8FeCHOECEcFHYERphXLaTUGz5OZ9FJH4-1aRus66Bo4-VFWw0tta_g0c2E5k1EGA--DW3-1BjbetfBFRji1n8bDBxudnrmu9lYegJ1GLoI5_L33wdvN9evkLps-3t5PLqeZ5jmLmeSsYKkfUbpQBhupKlqSVB41RDUqV4XmpuKS1GVFa5peUY2IrFBJc46VpvvgdMhdevexMiGK1gZtFgvZGbcKoqAE4ZzzBJ78A-du5bvUTWCWI5JzUqJEnQ2U9i4Ebxqx9LaV_ktgJPqZRZpZsF5TnOjj38yVak29YYddk381-PMQ5bv586WPVi9Mn4UrXvZ5fDj62I2dPkWYjn4DXCWPBg</recordid><startdate>1992</startdate><enddate>1992</enddate><creator>FUJIMOTO, Sadaki</creator><creator>MURAKAMI, Kazuki</creator><creator>HOSODA, Takashi</creator><creator>YAMAMOTO, Yuusuke</creator><creator>WATANABE, Katsuichi</creator><creator>MORINAKA, Yoshinori</creator><creator>OHARA, Akira</creator><general>The Pharmaceutical Society of Japan</general><general>Japan Science and Technology Agency</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>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>1992</creationdate><title>Characterization of Cationic Acid Phosphatase Isozyme from Rat Liver Mitochondria</title><author>FUJIMOTO, Sadaki ; MURAKAMI, Kazuki ; HOSODA, Takashi ; YAMAMOTO, Yuusuke ; WATANABE, Katsuichi ; MORINAKA, Yoshinori ; OHARA, Akira</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c564t-a54740002bc7be1eab93821340f2bfb6b7c5e95a2d893d30f20d02a9083651bc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>acid phosphatase</topic><topic>Acid Phosphatase - antagonists & inhibitors</topic><topic>Acid Phosphatase - chemistry</topic><topic>Acid Phosphatase - metabolism</topic><topic>Animals</topic><topic>Cations</topic><topic>Enzyme Activation</topic><topic>Isoelectric Point</topic><topic>Isoenzymes - antagonists & inhibitors</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - metabolism</topic><topic>Male</topic><topic>mitochondria</topic><topic>Mitochondria, Liver - enzymology</topic><topic>Molecular Weight</topic><topic>protein phosphatase</topic><topic>rat liver</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>FUJIMOTO, Sadaki</creatorcontrib><creatorcontrib>MURAKAMI, Kazuki</creatorcontrib><creatorcontrib>HOSODA, Takashi</creatorcontrib><creatorcontrib>YAMAMOTO, Yuusuke</creatorcontrib><creatorcontrib>WATANABE, Katsuichi</creatorcontrib><creatorcontrib>MORINAKA, Yoshinori</creatorcontrib><creatorcontrib>OHARA, Akira</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Chemical & pharmaceutical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>FUJIMOTO, Sadaki</au><au>MURAKAMI, Kazuki</au><au>HOSODA, Takashi</au><au>YAMAMOTO, Yuusuke</au><au>WATANABE, Katsuichi</au><au>MORINAKA, Yoshinori</au><au>OHARA, Akira</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of Cationic Acid Phosphatase Isozyme from Rat Liver Mitochondria</atitle><jtitle>Chemical & pharmaceutical bulletin</jtitle><addtitle>Chem. Pharm. Bull.</addtitle><date>1992</date><risdate>1992</risdate><volume>40</volume><issue>5</issue><spage>1231</spage><epage>1235</epage><pages>1231-1235</pages><issn>0009-2363</issn><eissn>1347-5223</eissn><abstract>Acid phosphatase isozyme was highly purified from rat liver mitochondrial fraction. The enzyme showed an isoelectric point value of above 9.5 on isoelectric focusing, and the apparent molecular weight was estimated to be 32000 by Sephadex G-100 gel filtration or 16000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme catalyzed the hydrolysis of adenosine 5'-triphosphate, adenosine 5'-diphosphate, thiamine pyrophosphate, inorganic pyrophosphate, and phosphoproteion such as casein and phosvitin, but not of several phosphomonoesters, except for p-nitrophenyl phosphate and o-phosphotyrosine. The enzyme was not inhibited by L-(+)-tartrate, and was significantly activated by Fe2+ and reducing agents such as ascorbic acid, L-cysteine, and dithiothreitol. The enzyme was found to be distributed in various rat tissues including liver, spleen, kidney, small intestine, lung, stomach, brain and beart, but not in skeletal muscle.</abstract><cop>Japan</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>1394639</pmid><doi>10.1248/cpb.40.1231</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Chemical and Pharmaceutical Bulletin, 1992/05/25, Vol.40(5), pp.1231-1235 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Free Full-Text Journals in Chemistry |
| subjects | acid phosphatase Acid Phosphatase - antagonists & inhibitors Acid Phosphatase - chemistry Acid Phosphatase - metabolism Animals Cations Enzyme Activation Isoelectric Point Isoenzymes - antagonists & inhibitors Isoenzymes - chemistry Isoenzymes - metabolism Male mitochondria Mitochondria, Liver - enzymology Molecular Weight protein phosphatase rat liver Rats Rats, Wistar Substrate Specificity |
| title | Characterization of Cationic Acid Phosphatase Isozyme from Rat Liver Mitochondria |
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