Localization of bovine liver aldehyde dehydrogenase isozymes and their immunological properties
Evidence supporting the existence of three aldehyde dehydrogenases in bovine liver has been confirmed and the immunological properties of these isozymes have been compared. 1. The cytoplasmic and mitochondrial aldehyde dehydrogenases were distinguished in size by subjecting the bovine liver crude ex...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1981-04, Vol.89 (4), p.1223-1229 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Kitabatake, N Sasaki, R Chiba, H |
| description | Evidence supporting the existence of three aldehyde dehydrogenases in bovine liver has been confirmed and the immunological properties of these isozymes have been compared. 1. The cytoplasmic and mitochondrial aldehyde dehydrogenases were distinguished in size by subjecting the bovine liver crude extract to Sephadex G-150 chromatog-raphy. The molecular weight of the cytoplasmic aldehyde dehydrogenase was determined to be 230, 000 daltons, larger than the mitochondrial enzyme by approximately 15, 000 daltons. 2. Submitochondrial fractionation indicated that the mitochondrial aldehyde dehydrogenase was located in the intermembrane space. 3. Anti-mitochondrial aldehyde dehydrogenase antibody from rabbit gave an im-munoreaction line not only with the mitochondrial enzyme but also with the cytoplasmic enzyme, and inhibited the activity of both enzymes. The anti-cytoplasmic aldehyde dehydrogenase antibody reacted with the cytoplasmic enzyme but had no effect on the mitochondrial enzyme. Neither antibody reacted with the micro-somal aldehyde dehydrogenase solubilized with sodium deoxycholate. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a133307 |
| format | Article |
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The cytoplasmic and mitochondrial aldehyde dehydrogenases were distinguished in size by subjecting the bovine liver crude extract to Sephadex G-150 chromatog-raphy. The molecular weight of the cytoplasmic aldehyde dehydrogenase was determined to be 230, 000 daltons, larger than the mitochondrial enzyme by approximately 15, 000 daltons. 2. Submitochondrial fractionation indicated that the mitochondrial aldehyde dehydrogenase was located in the intermembrane space. 3. Anti-mitochondrial aldehyde dehydrogenase antibody from rabbit gave an im-munoreaction line not only with the mitochondrial enzyme but also with the cytoplasmic enzyme, and inhibited the activity of both enzymes. The anti-cytoplasmic aldehyde dehydrogenase antibody reacted with the cytoplasmic enzyme but had no effect on the mitochondrial enzyme. 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The cytoplasmic and mitochondrial aldehyde dehydrogenases were distinguished in size by subjecting the bovine liver crude extract to Sephadex G-150 chromatog-raphy. The molecular weight of the cytoplasmic aldehyde dehydrogenase was determined to be 230, 000 daltons, larger than the mitochondrial enzyme by approximately 15, 000 daltons. 2. Submitochondrial fractionation indicated that the mitochondrial aldehyde dehydrogenase was located in the intermembrane space. 3. Anti-mitochondrial aldehyde dehydrogenase antibody from rabbit gave an im-munoreaction line not only with the mitochondrial enzyme but also with the cytoplasmic enzyme, and inhibited the activity of both enzymes. The anti-cytoplasmic aldehyde dehydrogenase antibody reacted with the cytoplasmic enzyme but had no effect on the mitochondrial enzyme. Neither antibody reacted with the micro-somal aldehyde dehydrogenase solubilized with sodium deoxycholate.</description><subject>Acetaldehyde - metabolism</subject><subject>Aldehyde Dehydrogenase</subject><subject>Aldehyde Oxidoreductases - immunology</subject><subject>animal physiology</subject><subject>Animals</subject><subject>Cattle</subject><subject>Cytoplasm - enzymology</subject><subject>Immunodiffusion</subject><subject>Isoenzymes - immunology</subject><subject>Liver - enzymology</subject><subject>Microsomes, Liver - enzymology</subject><subject>Molecular Weight</subject><subject>Submitochondrial Particles - enzymology</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kN1r2zAUxUVZ6bKuf8KYXrY3p_qwdO3HUbq1ENhDP9mLkO2rRJltZZIdkv71dZswuHC4nB_nHi4h3zibc1bKy7BzITbrMMbetmm-ruoVdnPLpZQMTsiMg9KZ0Ip_IDPGBM9KkT9_JJ9SWr-tQsozcqahKCZuRswi1Lb1L3bwoafB0SpsfY-09VuM1LYNrvYN0neJYYm9TUh9Ci_7DhO1fUOHFfpIfdeNfWjD0k9xdBPDBuPgMX0mp26qiRdHPScPP6_vr26yxe9ft1c_FpkTJQyZFKVWlldcFY1zOVcCSsirWuUWXQ26kqrRCqFCJ3gOOSqhSiglcyCZRiXPyfdD7nT634hpMJ1PNbat7TGMyYDMC9D6DfxyBMeqw8Zsou9s3JvjRyY_O_g-Dbj7b9v4d0IkKHPz_Mc8CfkEDB6NmPivB97ZYOwy-mQe7gTjchrOGGj5CkMWg2I</recordid><startdate>198104</startdate><enddate>198104</enddate><creator>Kitabatake, N</creator><creator>Sasaki, R</creator><creator>Chiba, H</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>198104</creationdate><title>Localization of bovine liver aldehyde dehydrogenase isozymes and their immunological properties</title><author>Kitabatake, N ; Sasaki, R ; Chiba, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f297t-32965a1b158dff41527974bc54aefc76b35d65e7bef21474e52597930f7306e53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Acetaldehyde - metabolism</topic><topic>Aldehyde Dehydrogenase</topic><topic>Aldehyde Oxidoreductases - immunology</topic><topic>animal physiology</topic><topic>Animals</topic><topic>Cattle</topic><topic>Cytoplasm - enzymology</topic><topic>Immunodiffusion</topic><topic>Isoenzymes - immunology</topic><topic>Liver - enzymology</topic><topic>Microsomes, Liver - enzymology</topic><topic>Molecular Weight</topic><topic>Submitochondrial Particles - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kitabatake, N</creatorcontrib><creatorcontrib>Sasaki, R</creatorcontrib><creatorcontrib>Chiba, H</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kitabatake, N</au><au>Sasaki, R</au><au>Chiba, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Localization of bovine liver aldehyde dehydrogenase isozymes and their immunological properties</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1981-04</date><risdate>1981</risdate><volume>89</volume><issue>4</issue><spage>1223</spage><epage>1229</epage><pages>1223-1229</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>Evidence supporting the existence of three aldehyde dehydrogenases in bovine liver has been confirmed and the immunological properties of these isozymes have been compared. 1. The cytoplasmic and mitochondrial aldehyde dehydrogenases were distinguished in size by subjecting the bovine liver crude extract to Sephadex G-150 chromatog-raphy. The molecular weight of the cytoplasmic aldehyde dehydrogenase was determined to be 230, 000 daltons, larger than the mitochondrial enzyme by approximately 15, 000 daltons. 2. Submitochondrial fractionation indicated that the mitochondrial aldehyde dehydrogenase was located in the intermembrane space. 3. Anti-mitochondrial aldehyde dehydrogenase antibody from rabbit gave an im-munoreaction line not only with the mitochondrial enzyme but also with the cytoplasmic enzyme, and inhibited the activity of both enzymes. The anti-cytoplasmic aldehyde dehydrogenase antibody reacted with the cytoplasmic enzyme but had no effect on the mitochondrial enzyme. 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| ispartof | Journal of biochemistry (Tokyo), 1981-04, Vol.89 (4), p.1223-1229 |
| issn | 0021-924X 1756-2651 |
| language | eng |
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| source | Oxford University Press Journals Digital Archive legacy; MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Free Full-Text Journals in Chemistry |
| subjects | Acetaldehyde - metabolism Aldehyde Dehydrogenase Aldehyde Oxidoreductases - immunology animal physiology Animals Cattle Cytoplasm - enzymology Immunodiffusion Isoenzymes - immunology Liver - enzymology Microsomes, Liver - enzymology Molecular Weight Submitochondrial Particles - enzymology |
| title | Localization of bovine liver aldehyde dehydrogenase isozymes and their immunological properties |
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