Hypertension, Vol 17, 923-929, Copyright © 1991 by American Heart Association
JH Ludens, MA Clark, DW DuCharme, DW Harris, BS Lutzke, F Mandel, WR Mathews, DM Sutter and JM Hamlyn
In previous reports, we described the isolation and characterization of an
endogenous digitalislike factor (EDLF). In this report, we describe a
unique combination of bioassay and large-scale purification methodology
that made possible the purification of sufficient quantities of this
inhibitor of Na+,K(+)-ATPase for structural analysis. Using an initial
XAD-2 extraction and preparative high- performance liquid chromatography
followed by a batch enzyme affinity extraction and two subsequent
semipreparative chromatographic steps, 300 l of human plasma was processed,
yielding 31 micrograms (53 nmol) of pure EDLF and representing purification
on a dry weight basis in excess of 0.6 billionfold. Four divergent pieces
of evidence, including chromatographic, mass spectrometric, immunoreactive,
and binding characteristics, suggested that the EDLF purified in the
present study was either ouabain or an isomer of ouabain. This material may
represent a plasma-borne, naturally occurring, selective, high-affinity
ligand for the digitalis binding site that may play a significant role in
the modulation of the sodium pump and thereby cellular electrolyte
homeostasis in humans.
ARTICLES
Purification of an endogenous digitalislike factor from human plasma for structural analysis
Upjohn Laboratories, Kalamazoo, Mich. 49001.
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