Characterization of NaK ATPase from the gills of the freshwater prawn Macrobrachium rosenbergii (de Man)

S. Stern; A. Borut; D. Cohen

doi:10.1016/0305-0491(84)90074-9

Characterization of NaK ATPase from the gills of the freshwater prawn Macrobrachium rosenbergii (de Man)

S. Stern^*, A. Borut, D. Cohen

^*Corresponding author for this work

Alexander Silberman Institute of Life Sciences

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

1. 1. The specific activity of Na-K ATPase was determined from the microsomal preparation of gills dissected from adult Macrobrachium rosenbergii. 2. 2. Maximal ATPase activity was achieved at a substrate concentration of 0.5 mM ATP. 3. 3. Optimal enzyme activity was obtained at pH of 7.5. 4. 4. The Arrhenius plot of Na-K ATPase activity revealed a marked discontinuity at 30°C. "Mg" ATPase activity did not exhibit a marked discontinuity. 5. 5. The E_a for Na-K ATPase and "Mg" ATPase was 14.6 kCal/mole and 9.31 kCal/mole respectively. Q₁₀ values for Na-K ATPase was 2.34 and for "Mg" ATPase 1.65. 6. 6. ATPase activity and gill homogenate protein concentration exhibited a linear relationship up to 130 μg protein/ml. 7. 7. Na-K ATPase activity was inhibited by 10^-3 M ouabain. It was equally inhibited by the removal of K⁺ from the reaction medium.

Original language	English
Pages (from-to)	47-50
Number of pages	4
Journal	Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
Volume	79
Issue number	1
DOIs	https://doi.org/10.1016/0305-0491(84)90074-9
State	Published - 1984

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title = "Characterization of NaK ATPase from the gills of the freshwater prawn Macrobrachium rosenbergii (de Man)",

abstract = "1. 1. The specific activity of Na-K ATPase was determined from the microsomal preparation of gills dissected from adult Macrobrachium rosenbergii. 2. 2. Maximal ATPase activity was achieved at a substrate concentration of 0.5 mM ATP. 3. 3. Optimal enzyme activity was obtained at pH of 7.5. 4. 4. The Arrhenius plot of Na-K ATPase activity revealed a marked discontinuity at 30°C. {"}Mg{"} ATPase activity did not exhibit a marked discontinuity. 5. 5. The Ea for Na-K ATPase and {"}Mg{"} ATPase was 14.6 kCal/mole and 9.31 kCal/mole respectively. Q10 values for Na-K ATPase was 2.34 and for {"}Mg{"} ATPase 1.65. 6. 6. ATPase activity and gill homogenate protein concentration exhibited a linear relationship up to 130 μg protein/ml. 7. 7. Na-K ATPase activity was inhibited by 10-3 M ouabain. It was equally inhibited by the removal of K+ from the reaction medium.",

author = "S. Stern and A. Borut and D. Cohen",

year = "1984",

doi = "10.1016/0305-0491(84)90074-9",

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T1 - Characterization of NaK ATPase from the gills of the freshwater prawn Macrobrachium rosenbergii (de Man)

AU - Stern, S.

AU - Borut, A.

AU - Cohen, D.

PY - 1984

Y1 - 1984

N2 - 1. 1. The specific activity of Na-K ATPase was determined from the microsomal preparation of gills dissected from adult Macrobrachium rosenbergii. 2. 2. Maximal ATPase activity was achieved at a substrate concentration of 0.5 mM ATP. 3. 3. Optimal enzyme activity was obtained at pH of 7.5. 4. 4. The Arrhenius plot of Na-K ATPase activity revealed a marked discontinuity at 30°C. "Mg" ATPase activity did not exhibit a marked discontinuity. 5. 5. The Ea for Na-K ATPase and "Mg" ATPase was 14.6 kCal/mole and 9.31 kCal/mole respectively. Q10 values for Na-K ATPase was 2.34 and for "Mg" ATPase 1.65. 6. 6. ATPase activity and gill homogenate protein concentration exhibited a linear relationship up to 130 μg protein/ml. 7. 7. Na-K ATPase activity was inhibited by 10-3 M ouabain. It was equally inhibited by the removal of K+ from the reaction medium.

AB - 1. 1. The specific activity of Na-K ATPase was determined from the microsomal preparation of gills dissected from adult Macrobrachium rosenbergii. 2. 2. Maximal ATPase activity was achieved at a substrate concentration of 0.5 mM ATP. 3. 3. Optimal enzyme activity was obtained at pH of 7.5. 4. 4. The Arrhenius plot of Na-K ATPase activity revealed a marked discontinuity at 30°C. "Mg" ATPase activity did not exhibit a marked discontinuity. 5. 5. The Ea for Na-K ATPase and "Mg" ATPase was 14.6 kCal/mole and 9.31 kCal/mole respectively. Q10 values for Na-K ATPase was 2.34 and for "Mg" ATPase 1.65. 6. 6. ATPase activity and gill homogenate protein concentration exhibited a linear relationship up to 130 μg protein/ml. 7. 7. Na-K ATPase activity was inhibited by 10-3 M ouabain. It was equally inhibited by the removal of K+ from the reaction medium.

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Characterization of NaK ATPase from the gills of the freshwater prawn Macrobrachium rosenbergii (de Man)

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