The susceptibility of the glycoprotein from the purified (Na+, K+)-activated adenosine triphosphatase to tryptic and chymotryptic degradation with and without Na+ and K+
- 1 May 1976
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 434 (1) , 258-264
- https://doi.org/10.1016/0005-2795(76)90057-x
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Studies on the characterization of the sodium—Potassium transport adenosine triphosphataseArchives of Biochemistry and Biophysics, 1974
- The Sodium-Potassium AdenosinetriphosphataseAnnual Review of Biochemistry, 1974
- Studies on the characterization of the sodium—potassium transport adenosinetriphosphataseArchives of Biochemistry and Biophysics, 1973
- Studies on the Characterization of the Sodium-Potassium Transport Adenosine TriphosphatasePublished by Elsevier ,1973
- Asymmetric interaction of inside-out and right-side-out erythrocyte membrane vesicles with ouabainBiochimica et Biophysica Acta (BBA) - Biomembranes, 1973
- Studies on the Characterization of the Sodium-Potassium Transport Adenosine TriphosphatasePublished by Elsevier ,1971
- Membrane enzyme systems molecular size determinations by radiation inactivationBiochimica et Biophysica Acta (BBA) - Biomembranes, 1968
- Studies on sodium-potassium-activated adenosinetriphosphatase. V. Correlation of enzyme activity with cation flux in six tissuesArchives of Biochemistry and Biophysics, 1963
- The asymmetrical stimulation of a membrane adenosine triphosphatase in relation to active cation transportBiochemical Journal, 1962
- Adenosinetriphosphatase activity and the active movements of alkali metal ionsThe Journal of Physiology, 1961