Isolation and characterization of lectins from stem and leaves of Korean mistletoe (Viscum album var.coloratum) by affinity chromatography

1997 ◽  
Vol 20 (4) ◽  
pp. 306-312 ◽  
Author(s):  
Won-Bong Park ◽  
Seon-Kyu Han ◽  
Myung-Hwan Lee ◽  
Kwang-Ho Han
Keyword(s):  
Affinity Chromatography ◽  
Viscum Album ◽  
Korean Mistletoe ◽  
Isolation And Characterization

scholarly journals Isolation and characterization of glyoxylate dehydrogenase from the fungus Sclerotium rolfsii

1984 ◽  
Vol 218 (1) ◽  
pp. 113-118 ◽  
Author(s):  
A J Balmforth ◽  
A Thomson
Keyword(s):  
Affinity Chromatography ◽  
Active Site ◽  
Sclerotium Rolfsii ◽  
Thiol Group ◽  
Isolation And Characterization ◽  
Crude Extracts ◽  
Nad Oxidoreductase ◽  
Inhibition Studies ◽  
Dye Affinity Chromatography

Glyoxylate dehydrogenase (glyoxylate: NAD+ oxidoreductase) was purified 600-fold in three steps from crude extracts of the fungus Sclerotium rolfsii (Corticium rolfsii Curzi). Two of the purification steps involved dye-affinity chromatography. The enzyme is a tetramer of Mr 250 000, with identical subunits of Mr 57 000. Inhibition studies suggest that there is one essential thiol group per active site.

scholarly journals Isolation and characterization of a digoxin-like immunoreactive substance from human urine by affinity chromatography

1997 ◽  
Vol 43 (8) ◽  
pp. 1416-1420 ◽  
Author(s):  
Claudio De Angelis ◽  
Massimiliano Riscazzi ◽  
Riccardo Salvini ◽  
Alfonso Piccoli ◽  
Claudio Ferri ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Human Urine ◽  
Biological Fluids ◽  
Active Material ◽  
Reversed Phase ◽  
Cross Reactivity ◽  
Linear Gradient ◽  
Isolation And Characterization ◽  
Dog Kidney

Abstract A series of observations has suggested that one or more digoxin-like immunoreactive substances (DLIS) in biological fluids is able to cross-react with the antidigoxin antibody. Whether this substance is the endogenous inhibitor of Na+/K+ ATPase has not been well established. The aim of this study was to identify and characterize DLIS from human urine. Treated urine from healthy men was run on an affinity chromatography column at a flow rate of 1 mL/min in which the ligand was an antibody (antiserum) to digoxin. Eluates from affinity chromatography were applied onto analytical reversed-phase HPLC. The active material was eluted with a linear gradient of acetonitrile (from 350 to 650 mL/L) and water. A second step in HPLC was carried out isocratically with 280 mL/L acetonitrile in water. We found a single peak showing cross-reactivity with antidigoxin antibody as measured by RIA. It showed the same retention time as that of a digoxin calibrator. This highly purified substance is able to displace [3H]ouabain from dog kidney-derived Na+/K+ ATPase, to inhibit Na+/K+ ATPase activity as measured by the86Rb+ uptake in red blood cells and by coupled enzyme assay. Our results are consistent with the hypothesis that DLIS, as isolated by this particular digoxin antibody, is a single substance and an inhibitor of Na+/K+ ATPase.

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