## Abstract (Na ^+^K)βactivated ATPase activity from gills of yearling spring chinook was examined using a new rapid assay method. Characterization of the enzyme activity was performed. Optimal activity was obtained at pH 7.2 in the presence of 240 mM NaCl, 120 mM KCl, 20 mM MgCl~2~ and 10 mM Na~2~
β¦ LIBER β¦
Purification of cardiac (Na+,K+)-activated adenosine triphosphatase from rat
β Scribed by Takahide Watanabe; Yuko Tawada; Munekazu Shigekawa
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 436 KB
- Volume
- 175
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A procedure is described for preparation of highly active (Na+,K+)-ATPax from rat heart which has a specific activity of 200-600 amol PJmg/h. The procedure is simple and can be applied to small amounts of heart muscle. (-1 g). The ATPase activity was more than 90% sensitive to ouahain (at concentrations up to 1 mM). The ouabain sensitivity is biphasic with about 20% of the ATPase activity being inhibited at -3 X lo-' M ouabain. Q 1988 Academic Pits, Inc.
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