{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T10:39:01Z","timestamp":1773657541335,"version":"3.50.1"},"reference-count":0,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[1975,10,1]],"date-time":"1975-10-01T00:00:00Z","timestamp":181353600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[1975,10]]},"abstract":"<jats:p>1. [3H]ouabain binding to human erythrocyte membranes is a time\u2010 and temperature\u2010dependent process. The association of ouabain to the membrane\u2010bound receptor follows second\u2010order kinetics, while the dissociation is a monomolecular reaction. An association rate constant of 4\u20106 x 10(4) M\u20101 sec\u20101 and a dissociation rate constant of 1\u20104 x 10(\u20104) sec\u20101 were measured at 37 degrees C. The dissociation constant calculated from these data agrees with that determined from equilibrium binding experiments. There is only one type of ouabain binding sites with high affinity for the drug as reflected by the low dissociation constant of 0\u201028 x 10(\u20108) M. 2. The dissociation constants of the ouabain\u2010receptor complexes from human erythrocyte and cardiac membranes are identical. 3. The maximal number of membrane\u2010bound ouabain binding sites was measured from equilibrium binding experiments as 288 +\/\u2010 28 per single erythrocyte. Thus one receptor site corresponds to less than 1 mum2 of the membrane, provided the receptors are diffusely distributed on the surface of the membrane. 4. Neither the maximal number of ouabain receptors nor the affinity for the drug changes with the age or sex of the blood donor. 5. A maximal transport capacity for sodium of 5\u20106 m\u2010equiv\/hr.1. is calculated from the number of receptor sites per erythrocyte and from the turn\u2010over number of the (Na+ + K+)\u2010ATPase.<\/jats:p>","DOI":"10.1113\/jphysiol.1975.sp011115","type":"journal-article","created":{"date-parts":[[2014,12,19]],"date-time":"2014-12-19T09:28:34Z","timestamp":1418981314000},"page":"671-682","source":"Crossref","is-referenced-by-count":75,"title":["Quantitative aspects of ouabain binding to human erythrocyte and cardiac membranes."],"prefix":"10.1113","volume":"251","author":[{"given":"E","family":"Erdmann","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"W","family":"Hasse","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[1975,10]]},"container-title":["The Journal of Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1113%2Fjphysiol.1975.sp011115","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/physoc.onlinelibrary.wiley.com\/doi\/pdf\/10.1113\/jphysiol.1975.sp011115","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,5]],"date-time":"2023-11-05T04:10:32Z","timestamp":1699157432000},"score":1,"resource":{"primary":{"URL":"https:\/\/physoc.onlinelibrary.wiley.com\/doi\/10.1113\/jphysiol.1975.sp011115"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1975,10]]},"references-count":0,"journal-issue":{"issue":"3","published-print":{"date-parts":[[1975,10]]}},"alternative-id":["10.1113\/jphysiol.1975.sp011115"],"URL":"https:\/\/doi.org\/10.1113\/jphysiol.1975.sp011115","archive":["Portico"],"relation":{},"ISSN":["0022-3751","1469-7793"],"issn-type":[{"value":"0022-3751","type":"print"},{"value":"1469-7793","type":"electronic"}],"subject":[],"published":{"date-parts":[[1975,10]]}}}