Add time:08/16/2019         Source:sciencedirect.com

1.(1) [3H]g-strophanthin (ouabain) binding to (Na+ + K+)- activated ATPase from ox brain was studied as a function of the Pi concentration with the (Mg2+ +Pi)-facilitated pathway. Scatchard-type plots of bound versus bound/free g-strophanthin at equilibrium of binding resulted in curved lines. The non-linearity was most easily seen at low Pi concentration or after addition of the nucleotide analogue β,γ-methyl-eneadenosine triphosphate (ADPCP) or suramin at high Pi concentration.2.(2) The curved lines obtained with (Mg2+ +Pi)-supported g-strophanthin binding are converted to straight lines at a certain, not very high K+ concentration. This effect seems specific for K+ and is apparently not due to a delay of the time of equilibrium.3.(3) The experiments are explained by assuming the existence of two (or more) populations of enzymes with different affinities for substrates and ligands affecting g-strophanthin binding. The sites with apparently high affinity for g-strophanthin may be less dependent on Pi for g-strophanthin binding or they may have a higher affinity for Pi. On the other hand, they are more affected by K+ such that all enzyme sites exhibit homogeneity with respect to g-strophanthin affinity after addition of K+.

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