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
Hauptverfasser: Takeda, Kazuo, Noguchi, Shunsuke, Sugino, Atsuko, Kawamura, Masaru
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container_title FEBS letters
container_volume 238
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
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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. 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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. 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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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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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