[Isolation of steroid-binding proteins on new affinity adsorbents].
Steroid-binding proteins of human blood are extracted and investigated on corticosteroid-hydrazide-oxypropyl-adsorbents by the affinity chromatography. The role of structural changes in the matrix-spacer-ligand system for different types of adsorbents is studied as well as a dependence of sorption on pH and salt environment. A dependence of the protein sorption on the isolated hydrazide groups is revealed. It is shown that hydrocortisone displays the highest binding activity to the protein pool in the affinity electroimmunoassay while the substance S-Reichstein and its 16-alpha-methyl analog--the least one.
Kuznetsov
P V
PV
Demin
O A
OA
Kononenko
V Ia
VIa
Zinchuk
S F
SF
D000327:Adsorption; D002846:Chromatography, Affinity / Q000295:instrumentation; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007122:Immunoelectrophoresis; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D012965:Sodium Chloride; D013256:Steroids / Q000378:metabolism*
D010455:Peptides; D013256:Steroids; D012965:Sodium Chloride
Vydelenie steroidsviazyvaiushchikh belkov na novykh affinnykh adsorbentakh.