Studies on rat hepatic hydroxysteroid sulfotransferase--immunochemistry, development and pI variants
Rat hepatic hydroxysteroid sulfotransferase with sulfoconjugates androsterone (androsterone-sulfating sulfotransferase) is an oligomer consisting of several subunits with distinct pI values but with the same molecular mass (pI variants). N-terminal amino acid sequences of the pI variants are all ide...
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| Veröffentlicht in: | Chemico-biological interactions 1994-06, Vol.92 (1-3), p.15-24 |
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| container_title | Chemico-biological interactions |
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| creator | Homma, H Nakagome, I Kamakura, M Hirota, M Takahashi, M Matsui, M |
| description | Rat hepatic hydroxysteroid sulfotransferase with sulfoconjugates androsterone (androsterone-sulfating sulfotransferase) is an oligomer consisting of several subunits with distinct pI values but with the same molecular mass (pI variants). N-terminal amino acid sequences of the pI variants are all identical. The enzyme is exclusively present in the liver, in which its lobular localization is sex-dependent. The localization of the enzyme is markedly different from that of an isoenzyme of phenol sulfotransferase. In weanling and adult female rats, the relative abundance of the pI variants is different. During development from weanling stage to adulthood, the amounts of acidic variants increase, whereas the relative levels of alkaline variants remain constant. |
| doi_str_mv | 10.1016/0009-2797(94)90049-3 |
| format | Article |
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N-terminal amino acid sequences of the pI variants are all identical. The enzyme is exclusively present in the liver, in which its lobular localization is sex-dependent. The localization of the enzyme is markedly different from that of an isoenzyme of phenol sulfotransferase. In weanling and adult female rats, the relative abundance of the pI variants is different. During development from weanling stage to adulthood, the amounts of acidic variants increase, whereas the relative levels of alkaline variants remain constant.</description><identifier>ISSN: 0009-2797</identifier><identifier>DOI: 10.1016/0009-2797(94)90049-3</identifier><identifier>PMID: 8033250</identifier><language>eng</language><publisher>Ireland</publisher><subject>Aging - metabolism ; Amino Acid Sequence ; Androsterone - metabolism ; Animals ; Female ; Immunohistochemistry ; Isoelectric Point ; Isoenzymes - chemistry ; Isoenzymes - metabolism ; Kidney - enzymology ; Liver - enzymology ; Male ; Molecular Sequence Data ; Molecular Weight ; Rats ; Sulfotransferases - chemistry ; Sulfotransferases - metabolism ; Tissue Distribution</subject><ispartof>Chemico-biological interactions, 1994-06, Vol.92 (1-3), p.15-24</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c327t-47db3b7b7b1fa8d6d09cb6e241923aae52553fd3d6d8f0c39f3c297c0fa17e063</citedby><cites>FETCH-LOGICAL-c327t-47db3b7b7b1fa8d6d09cb6e241923aae52553fd3d6d8f0c39f3c297c0fa17e063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8033250$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Homma, H</creatorcontrib><creatorcontrib>Nakagome, I</creatorcontrib><creatorcontrib>Kamakura, M</creatorcontrib><creatorcontrib>Hirota, M</creatorcontrib><creatorcontrib>Takahashi, M</creatorcontrib><creatorcontrib>Matsui, M</creatorcontrib><title>Studies on rat hepatic hydroxysteroid sulfotransferase--immunochemistry, development and pI variants</title><title>Chemico-biological interactions</title><addtitle>Chem Biol Interact</addtitle><description>Rat hepatic hydroxysteroid sulfotransferase with sulfoconjugates androsterone (androsterone-sulfating sulfotransferase) is an oligomer consisting of several subunits with distinct pI values but with the same molecular mass (pI variants). N-terminal amino acid sequences of the pI variants are all identical. The enzyme is exclusively present in the liver, in which its lobular localization is sex-dependent. The localization of the enzyme is markedly different from that of an isoenzyme of phenol sulfotransferase. In weanling and adult female rats, the relative abundance of the pI variants is different. During development from weanling stage to adulthood, the amounts of acidic variants increase, whereas the relative levels of alkaline variants remain constant.</description><subject>Aging - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Androsterone - metabolism</subject><subject>Animals</subject><subject>Female</subject><subject>Immunohistochemistry</subject><subject>Isoelectric Point</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - metabolism</subject><subject>Kidney - enzymology</subject><subject>Liver - enzymology</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Rats</subject><subject>Sulfotransferases - chemistry</subject><subject>Sulfotransferases - metabolism</subject><subject>Tissue Distribution</subject><issn>0009-2797</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1LxDAQhnNQ1nX1HyjkJApWp02_cpTFj4UFD-o5pMmErbRNTdLF_nu77rLMYZiZ930ZHkKuYniIIc4fAYBHScGLW57ecYCUR-yEzI_rM3Lu_fc0QpLCjMxKYCzJYE70Rxh0jZ7ajjoZ6AZ7GWpFN6N29nf0AZ2tNfVDY2xwsvMGnfQYRXXbDp1VG2xrH9x4TzVusbF9i12gstO0X9GtdLXsgr8gp0Y2Hi8PfUG-Xp4_l2_R-v11tXxaR4olRYjSQlesKqaKjSx1roGrKsckjXnCpMQsyTJmNJsupQHFuGEq4YUCI-MCIWcLcrPP7Z39GdAHMT2nsGlkh3bwoshzSMs4m4TpXqic9d6hEb2rW-lGEYPYARU7cmJHTvBU_AMVbLJdH_KHqkV9NB1osj_ibXXU</recordid><startdate>19940601</startdate><enddate>19940601</enddate><creator>Homma, H</creator><creator>Nakagome, I</creator><creator>Kamakura, M</creator><creator>Hirota, M</creator><creator>Takahashi, M</creator><creator>Matsui, M</creator><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>19940601</creationdate><title>Studies on rat hepatic hydroxysteroid sulfotransferase--immunochemistry, development and pI variants</title><author>Homma, H ; Nakagome, I ; Kamakura, M ; Hirota, M ; Takahashi, M ; Matsui, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c327t-47db3b7b7b1fa8d6d09cb6e241923aae52553fd3d6d8f0c39f3c297c0fa17e063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Aging - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Androsterone - metabolism</topic><topic>Animals</topic><topic>Female</topic><topic>Immunohistochemistry</topic><topic>Isoelectric Point</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - metabolism</topic><topic>Kidney - enzymology</topic><topic>Liver - enzymology</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Rats</topic><topic>Sulfotransferases - chemistry</topic><topic>Sulfotransferases - metabolism</topic><topic>Tissue Distribution</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Homma, H</creatorcontrib><creatorcontrib>Nakagome, I</creatorcontrib><creatorcontrib>Kamakura, M</creatorcontrib><creatorcontrib>Hirota, M</creatorcontrib><creatorcontrib>Takahashi, M</creatorcontrib><creatorcontrib>Matsui, M</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>Chemico-biological interactions</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Homma, H</au><au>Nakagome, I</au><au>Kamakura, M</au><au>Hirota, M</au><au>Takahashi, M</au><au>Matsui, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Studies on rat hepatic hydroxysteroid sulfotransferase--immunochemistry, development and pI variants</atitle><jtitle>Chemico-biological interactions</jtitle><addtitle>Chem Biol Interact</addtitle><date>1994-06-01</date><risdate>1994</risdate><volume>92</volume><issue>1-3</issue><spage>15</spage><epage>24</epage><pages>15-24</pages><issn>0009-2797</issn><abstract>Rat hepatic hydroxysteroid sulfotransferase with sulfoconjugates androsterone (androsterone-sulfating sulfotransferase) is an oligomer consisting of several subunits with distinct pI values but with the same molecular mass (pI variants). N-terminal amino acid sequences of the pI variants are all identical. The enzyme is exclusively present in the liver, in which its lobular localization is sex-dependent. The localization of the enzyme is markedly different from that of an isoenzyme of phenol sulfotransferase. In weanling and adult female rats, the relative abundance of the pI variants is different. During development from weanling stage to adulthood, the amounts of acidic variants increase, whereas the relative levels of alkaline variants remain constant.</abstract><cop>Ireland</cop><pmid>8033250</pmid><doi>10.1016/0009-2797(94)90049-3</doi><tpages>10</tpages></addata></record> |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Aging - metabolism Amino Acid Sequence Androsterone - metabolism Animals Female Immunohistochemistry Isoelectric Point Isoenzymes - chemistry Isoenzymes - metabolism Kidney - enzymology Liver - enzymology Male Molecular Sequence Data Molecular Weight Rats Sulfotransferases - chemistry Sulfotransferases - metabolism Tissue Distribution |
| title | Studies on rat hepatic hydroxysteroid sulfotransferase--immunochemistry, development and pI variants |
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