Functional activity of oligosaccharide-deficient (Na,K)ATPase expressed in Xenopus oocytes
(Na,K)ATPase from Torpedo californica was expressed in Xenopus laevis oocytes in the presence of tunicamycin by injecting mRNAs for the α- and β-subunits derived from the cloned cDNAs into the oocytes. The oligosaccharide-deficient ATPase thus synthesized was transported to the oocytes plasma membra...
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Veröffentlicht in: | FEBS letters 1988-09, Vol.238 (1), p.201-204 |
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creator | Takeda, Kazuo Noguchi, Shunsuke Sugino, Atsuko Kawamura, Masaru |
description | (Na,K)ATPase from
Torpedo californica was expressed in
Xenopus laevis oocytes in the presence of tunicamycin by injecting mRNAs for the α- and β-subunits derived from the cloned cDNAs into the oocytes. The oligosaccharide-deficient ATPase thus synthesized was transported to the oocytes plasma membrane, where it exhibited virtually the same ATPase activity, ouabain-binding capacity and
86Rb
+ transport activity as the fully glycosylated enzyme. We conclude that the oligosaccharide chains on the β-subunit has no effect on the catalytic activities of (Na,K)ATPase. |
doi_str_mv | 10.1016/0014-5793(88)80256-4 |
format | Article |
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Torpedo californica was expressed in
Xenopus laevis oocytes in the presence of tunicamycin by injecting mRNAs for the α- and β-subunits derived from the cloned cDNAs into the oocytes. The oligosaccharide-deficient ATPase thus synthesized was transported to the oocytes plasma membrane, where it exhibited virtually the same ATPase activity, ouabain-binding capacity and
86Rb
+ transport activity as the fully glycosylated enzyme. We conclude that the oligosaccharide chains on the β-subunit has no effect on the catalytic activities of (Na,K)ATPase.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(88)80256-4</identifier><identifier>PMID: 2844594</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>(Na + + K +)ATPase ; (Na,K)ATPase, sodium- and potassium-dependent adenosine triphosphatase ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; Female ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - genetics ; Hydrolases ; Kinetics ; Oligosaccharide chain ; oligosaccharides ; Oligosaccharides - genetics ; oocytes ; Oocytes - drug effects ; Oocytes - metabolism ; PMSF, phenylmethanesulfonyl fluoride ; Protein Biosynthesis - drug effects ; RNA, Messenger - genetics ; Sodium-Potassium-Exchanging ATPase - genetics ; Sodium-Potassium-Exchanging ATPase - metabolism ; Torpedo ; Tunicamycin ; Tunicamycin - pharmacology ; Xenopus laevis ; Xenopus oocyte</subject><ispartof>FEBS letters, 1988-09, Vol.238 (1), p.201-204</ispartof><rights>1988</rights><rights>FEBS Letters 238 (1988) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5264-21ade90cdcac99dfdc0bf484cf240003a0dd7ab018f79cb0321e2ba87bab63463</citedby><cites>FETCH-LOGICAL-c5264-21ade90cdcac99dfdc0bf484cf240003a0dd7ab018f79cb0321e2ba87bab63463</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(88)80256-4$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6961993$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2844594$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takeda, Kazuo</creatorcontrib><creatorcontrib>Noguchi, Shunsuke</creatorcontrib><creatorcontrib>Sugino, Atsuko</creatorcontrib><creatorcontrib>Kawamura, Masaru</creatorcontrib><title>Functional activity of oligosaccharide-deficient (Na,K)ATPase expressed in Xenopus oocytes</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>(Na,K)ATPase from
Torpedo californica was expressed in
Xenopus laevis oocytes in the presence of tunicamycin by injecting mRNAs for the α- and β-subunits derived from the cloned cDNAs into the oocytes. The oligosaccharide-deficient ATPase thus synthesized was transported to the oocytes plasma membrane, where it exhibited virtually the same ATPase activity, ouabain-binding capacity and
86Rb
+ transport activity as the fully glycosylated enzyme. We conclude that the oligosaccharide chains on the β-subunit has no effect on the catalytic activities of (Na,K)ATPase.</description><subject>(Na + + K +)ATPase</subject><subject>(Na,K)ATPase, sodium- and potassium-dependent adenosine triphosphatase</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - genetics</subject><subject>Hydrolases</subject><subject>Kinetics</subject><subject>Oligosaccharide chain</subject><subject>oligosaccharides</subject><subject>Oligosaccharides - genetics</subject><subject>oocytes</subject><subject>Oocytes - drug effects</subject><subject>Oocytes - metabolism</subject><subject>PMSF, phenylmethanesulfonyl fluoride</subject><subject>Protein Biosynthesis - drug effects</subject><subject>RNA, Messenger - genetics</subject><subject>Sodium-Potassium-Exchanging ATPase - genetics</subject><subject>Sodium-Potassium-Exchanging ATPase - metabolism</subject><subject>Torpedo</subject><subject>Tunicamycin</subject><subject>Tunicamycin - pharmacology</subject><subject>Xenopus laevis</subject><subject>Xenopus oocyte</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkcFu1DAQhi0EKkvhDUDKAaFWasBOnMS-IJWqWyoq4FAkxMVyxmMwysaLnZTu29furvZYOHk88_ufmc-EvGT0LaOsfUcp42XTyfpIiGNBq6Yt-SOyYKKry5q34jFZ7CVPybMYf9N0F0wekINKcN5IviA_lvMIk_OjHgqdghs3bQpvCz-4nz5qgF86OIOlQevA4TgVR5_1yafj0-uvOmKBt-uAMaIp3Fh8x9Gv51h4D5sJ43PyxOoh4ovdeUi-Lc-vzz6WV18uLs9Or0poqpaXFdMGJQUDGqQ01gDtLRccbMXTwLWmxnS6T5PbTkJP64ph1WvR9bpv0571IXmz9V0H_2fGOKmVi4DDoEf0c1Sd4E1iwP8pZE3dVIzXSci3Qgg-xoBWrYNb6bBRjKrMXmWwKoNVQqh79ir7v9r5z_0Kzf7RDnaqv97VdQQ92KBHcHEva2XLpMzdl1vZXzfg5r9aq-X5hyoXcl6I-2zu935rhIn-jcOgYv5CQOMCwqSMdw8vdAfsWbO7</recordid><startdate>19880926</startdate><enddate>19880926</enddate><creator>Takeda, Kazuo</creator><creator>Noguchi, Shunsuke</creator><creator>Sugino, Atsuko</creator><creator>Kawamura, Masaru</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19880926</creationdate><title>Functional activity of oligosaccharide-deficient (Na,K)ATPase expressed in Xenopus oocytes</title><author>Takeda, Kazuo ; Noguchi, Shunsuke ; Sugino, Atsuko ; Kawamura, Masaru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5264-21ade90cdcac99dfdc0bf484cf240003a0dd7ab018f79cb0321e2ba87bab63463</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>(Na + + K +)ATPase</topic><topic>(Na,K)ATPase, sodium- and potassium-dependent adenosine triphosphatase</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - genetics</topic><topic>Hydrolases</topic><topic>Kinetics</topic><topic>Oligosaccharide chain</topic><topic>oligosaccharides</topic><topic>Oligosaccharides - genetics</topic><topic>oocytes</topic><topic>Oocytes - drug effects</topic><topic>Oocytes - metabolism</topic><topic>PMSF, phenylmethanesulfonyl fluoride</topic><topic>Protein Biosynthesis - drug effects</topic><topic>RNA, Messenger - genetics</topic><topic>Sodium-Potassium-Exchanging ATPase - genetics</topic><topic>Sodium-Potassium-Exchanging ATPase - metabolism</topic><topic>Torpedo</topic><topic>Tunicamycin</topic><topic>Tunicamycin - pharmacology</topic><topic>Xenopus laevis</topic><topic>Xenopus oocyte</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takeda, Kazuo</creatorcontrib><creatorcontrib>Noguchi, Shunsuke</creatorcontrib><creatorcontrib>Sugino, Atsuko</creatorcontrib><creatorcontrib>Kawamura, Masaru</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takeda, Kazuo</au><au>Noguchi, Shunsuke</au><au>Sugino, Atsuko</au><au>Kawamura, Masaru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional activity of oligosaccharide-deficient (Na,K)ATPase expressed in Xenopus oocytes</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1988-09-26</date><risdate>1988</risdate><volume>238</volume><issue>1</issue><spage>201</spage><epage>204</epage><pages>201-204</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>(Na,K)ATPase from
Torpedo californica was expressed in
Xenopus laevis oocytes in the presence of tunicamycin by injecting mRNAs for the α- and β-subunits derived from the cloned cDNAs into the oocytes. The oligosaccharide-deficient ATPase thus synthesized was transported to the oocytes plasma membrane, where it exhibited virtually the same ATPase activity, ouabain-binding capacity and
86Rb
+ transport activity as the fully glycosylated enzyme. We conclude that the oligosaccharide chains on the β-subunit has no effect on the catalytic activities of (Na,K)ATPase.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>2844594</pmid><doi>10.1016/0014-5793(88)80256-4</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
subjects | (Na + + K +)ATPase (Na,K)ATPase, sodium- and potassium-dependent adenosine triphosphatase Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Enzymes and enzyme inhibitors Female Fundamental and applied biological sciences. Psychology Glycoproteins - genetics Hydrolases Kinetics Oligosaccharide chain oligosaccharides Oligosaccharides - genetics oocytes Oocytes - drug effects Oocytes - metabolism PMSF, phenylmethanesulfonyl fluoride Protein Biosynthesis - drug effects RNA, Messenger - genetics Sodium-Potassium-Exchanging ATPase - genetics Sodium-Potassium-Exchanging ATPase - metabolism Torpedo Tunicamycin Tunicamycin - pharmacology Xenopus laevis Xenopus oocyte |
title | Functional activity of oligosaccharide-deficient (Na,K)ATPase expressed in Xenopus oocytes |
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