A carrier enzyme basis for ammonium excretion in teleost gill. NH+4-stimulated Na-dependent ATPase activity in Opsanus beta

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Abstract

1. 1. Branchial Na+ K+-ATPase specific activity is some 20% greater in hyposahne adapted Opsanus beta than in SW specimens. 2. 2. Ouabain insensitive ATPase (Mg2+-ATPase) specific activities were similar, while whole body-activity differences in low salinity and SW adapted fish could be accounted for by the 30% difference in extractable gill protein. 3. 3. NH4+ ion was 15% more effective at dephosphorylation of the microsomal Na-dependent phosphoenzyme than either Rb+ or K+. and revealed a maximal ATPase affinity (Km = 0.2 mM) within the physiological range of blood [K+]. 4. 4. Similar properties as pH optima, ATP and Mg2+ Km's. ouabain sensitivity, percent recoveries and subcell distribution indicated that the NH+4-stimulation acts through the Na+ K+ -ATPase carrier enzyme and may be resonsible for the Na+/NH+4 exchange in Opsanu beta.

Original languageEnglish (US)
Pages (from-to)889-897
Number of pages9
JournalComparative Biochemistry and Physiology -- Part A: Physiology
Volume74
Issue number4
DOIs
StatePublished - Jan 1 1983

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Batrachoidiformes
Ouabain
Ammonium Compounds
Adenosine Triphosphatases
Ca(2+) Mg(2+)-ATPase
Salinity
Enzymes
Fishes
Adenosine Triphosphate
Ions
Fish
Blood
Recovery
Proteins
sodium-translocating ATPase

ASJC Scopus subject areas

  • Physiology
  • Biochemistry
  • Molecular Biology

Cite this

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title = "A carrier enzyme basis for ammonium excretion in teleost gill. NH+4-stimulated Na-dependent ATPase activity in Opsanus beta",
abstract = "1. 1. Branchial Na+ K+-ATPase specific activity is some 20{\%} greater in hyposahne adapted Opsanus beta than in SW specimens. 2. 2. Ouabain insensitive ATPase (Mg2+-ATPase) specific activities were similar, while whole body-activity differences in low salinity and SW adapted fish could be accounted for by the 30{\%} difference in extractable gill protein. 3. 3. NH4+ ion was 15{\%} more effective at dephosphorylation of the microsomal Na-dependent phosphoenzyme than either Rb+ or K+. and revealed a maximal ATPase affinity (Km = 0.2 mM) within the physiological range of blood [K+]. 4. 4. Similar properties as pH optima, ATP and Mg2+ Km's. ouabain sensitivity, percent recoveries and subcell distribution indicated that the NH+4-stimulation acts through the Na+ K+ -ATPase carrier enzyme and may be resonsible for the Na+/NH+4 exchange in Opsanu beta.",
author = "Charles Mallery",
year = "1983",
month = "1",
day = "1",
doi = "10.1016/0300-9629(83)90364-X",
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pages = "889--897",
journal = "Comparative Biochemistry & Physiology; A: Comparative Physiology",
issn = "1095-6433",
publisher = "Elsevier Inc.",
number = "4",

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TY - JOUR

T1 - A carrier enzyme basis for ammonium excretion in teleost gill. NH+4-stimulated Na-dependent ATPase activity in Opsanus beta

AU - Mallery, Charles

PY - 1983/1/1

Y1 - 1983/1/1

N2 - 1. 1. Branchial Na+ K+-ATPase specific activity is some 20% greater in hyposahne adapted Opsanus beta than in SW specimens. 2. 2. Ouabain insensitive ATPase (Mg2+-ATPase) specific activities were similar, while whole body-activity differences in low salinity and SW adapted fish could be accounted for by the 30% difference in extractable gill protein. 3. 3. NH4+ ion was 15% more effective at dephosphorylation of the microsomal Na-dependent phosphoenzyme than either Rb+ or K+. and revealed a maximal ATPase affinity (Km = 0.2 mM) within the physiological range of blood [K+]. 4. 4. Similar properties as pH optima, ATP and Mg2+ Km's. ouabain sensitivity, percent recoveries and subcell distribution indicated that the NH+4-stimulation acts through the Na+ K+ -ATPase carrier enzyme and may be resonsible for the Na+/NH+4 exchange in Opsanu beta.

AB - 1. 1. Branchial Na+ K+-ATPase specific activity is some 20% greater in hyposahne adapted Opsanus beta than in SW specimens. 2. 2. Ouabain insensitive ATPase (Mg2+-ATPase) specific activities were similar, while whole body-activity differences in low salinity and SW adapted fish could be accounted for by the 30% difference in extractable gill protein. 3. 3. NH4+ ion was 15% more effective at dephosphorylation of the microsomal Na-dependent phosphoenzyme than either Rb+ or K+. and revealed a maximal ATPase affinity (Km = 0.2 mM) within the physiological range of blood [K+]. 4. 4. Similar properties as pH optima, ATP and Mg2+ Km's. ouabain sensitivity, percent recoveries and subcell distribution indicated that the NH+4-stimulation acts through the Na+ K+ -ATPase carrier enzyme and may be resonsible for the Na+/NH+4 exchange in Opsanu beta.

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U2 - 10.1016/0300-9629(83)90364-X

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JF - Comparative Biochemistry & Physiology; A: Comparative Physiology

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