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W Schoner

Showing results (21-30 of 125) with videos related to

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Journal of Theoretical Biology|March 7, 1992
Investigation of subunit interactions by radiation inactivation: the case of Na+/K+-ATPaseE Buxbaum, W Schoner
Deutsche Medizinische Wochenschrift (1946)|December 11, 2008
[From Digitalis purpurea to toad skin. An historical view of digitalis-like mammalian hormones ]E Ritz, W Schoner
Verhandlungen Der Deutschen Gesellschaft Fur Kreislaufforschung|January 1, 1974
[Affinity of various structured cardiac glycosides, DPH and Ro 2-2985 to the receptor of cardiac glycosides]E Erdmann, W Schoner
Biochimica Et Biophysica Acta|January 5, 1983
Imidazole chloride and tris-chloride substitute for sodium chloride in inducing high-affinity AdoPP[NH]P binding to (Na+ + K+)-ATPaseG Rempeters, W Schoner
Verhandlungen Der Deutschen Gesellschaft Fur Kreislaufforschung|January 1, 1973
[Characterization of the strophantin receptor in the cell membranes from heart, kidney and brain]E Erdmann, W Schoner
Biochimica Et Biophysica Acta|December 22, 1973
Ouabain-receptor interactions in (Na+ + K+)-ATPase preparations. II. Effect of cations and nucleotides on rate constants and dissociation constantsE Erdmann, W Schoner
Biochimica Et Biophysica Acta|December 22, 1973
Ouabain-receptor interactions in (Na+ + K+)-ATPase preparations. 3. On the stability of the ouabain receptor against physical treatment, hydrolases and SH reagentsE Erdmann, W Schoner
Klinische Wochenschrift|August 1, 1974
[Properties of the receptor for cardiac glycosides (author's transl)]E Erdmann, W Schoner
European Journal of Biochemistry|January 30, 1991
Phosphate binding and ATP-binding sites coexist in Na+/K(+)-transporting ATPase, as demonstrated by the inactivating MgPO4 complex analogue Co(NH3)4PO4E Buxbaum, W Schoner
European Journal of Biochemistry|October 24, 1990
Blocking of Na+/K+ transport by the MgPO4 complex analogue Co(NH3)4PO4 leaves the Na+/Na(+)-exchange reaction of the sodium pump unaltered and shifts its high-affinity ATP-binding site to a Na(+)-like formE Buxbaum, W Schoner
Pageof 13

Showing results (21-30 of 125) with videos related to

Sort By:
Pageof 13
Journal of Theoretical Biology|March 7, 1992
Investigation of subunit interactions by radiation inactivation: the case of Na+/K+-ATPaseE Buxbaum, W Schoner
Deutsche Medizinische Wochenschrift (1946)|December 11, 2008
[From Digitalis purpurea to toad skin. An historical view of digitalis-like mammalian hormones ]E Ritz, W Schoner
Verhandlungen Der Deutschen Gesellschaft Fur Kreislaufforschung|January 1, 1974
[Affinity of various structured cardiac glycosides, DPH and Ro 2-2985 to the receptor of cardiac glycosides]E Erdmann, W Schoner
Biochimica Et Biophysica Acta|January 5, 1983
Imidazole chloride and tris-chloride substitute for sodium chloride in inducing high-affinity AdoPP[NH]P binding to (Na+ + K+)-ATPaseG Rempeters, W Schoner
Verhandlungen Der Deutschen Gesellschaft Fur Kreislaufforschung|January 1, 1973
[Characterization of the strophantin receptor in the cell membranes from heart, kidney and brain]E Erdmann, W Schoner
Biochimica Et Biophysica Acta|December 22, 1973
Ouabain-receptor interactions in (Na+ + K+)-ATPase preparations. II. Effect of cations and nucleotides on rate constants and dissociation constantsE Erdmann, W Schoner
Biochimica Et Biophysica Acta|December 22, 1973
Ouabain-receptor interactions in (Na+ + K+)-ATPase preparations. 3. On the stability of the ouabain receptor against physical treatment, hydrolases and SH reagentsE Erdmann, W Schoner
Klinische Wochenschrift|August 1, 1974
[Properties of the receptor for cardiac glycosides (author's transl)]E Erdmann, W Schoner
European Journal of Biochemistry|January 30, 1991
Phosphate binding and ATP-binding sites coexist in Na+/K(+)-transporting ATPase, as demonstrated by the inactivating MgPO4 complex analogue Co(NH3)4PO4E Buxbaum, W Schoner
European Journal of Biochemistry|October 24, 1990
Blocking of Na+/K+ transport by the MgPO4 complex analogue Co(NH3)4PO4 leaves the Na+/Na(+)-exchange reaction of the sodium pump unaltered and shifts its high-affinity ATP-binding site to a Na(+)-like formE Buxbaum, W Schoner
Pageof 13