Isolation of lactoferrin from whey by dye-affinity chromatography with Yellow HE-4R attached to chitosan mini-spheres

2014 ◽  
Vol 39 (1) ◽  
pp. 53-59 ◽  
Author(s):  
María Fernanda Baieli ◽  
Nicolás Urtasun ◽  
María Victoria Miranda ◽  
Osvaldo Cascone ◽  
Federico Javier Wolman
Keyword(s):  
Affinity Chromatography ◽  
Dye Affinity Chromatography

Polymer displacement in dye-affinity chromatography

1995 ◽  
Vol 710 (2) ◽  
pp. 259-266 ◽  
Author(s):  
Igor Yu. Galaev ◽  
Pär Arvidsson ◽  
Bo Mattiasson
Keyword(s):  
Affinity Chromatography ◽  
Dye Affinity Chromatography

Fungal pectic enzyme fractionation by dye affinity chromatography

1996 ◽  
Vol 10 (3) ◽  
pp. 211-214 ◽  
Author(s):  
Silvia A. Camperi ◽  
Mariano Grasselli ◽  
Osvaldo Cascone
Keyword(s):  
Affinity Chromatography ◽  
Pectic Enzyme ◽  
Dye Affinity Chromatography

Coated silica and its behaviour in dye-affinity chromatography

1991 ◽  
Vol 543 ◽  
pp. 9-16 ◽  
Author(s):  
Danica Mislovičová ◽  
Ivan Novák ◽  
Mikuláš Pašteka
Keyword(s):  
Affinity Chromatography ◽  
Dye Affinity Chromatography

Dye affinity chromatography of ricin subunits

1986 ◽  
Vol 6 (12) ◽  
pp. 1035-1040 ◽  
Author(s):  
Simonetta Sperti ◽  
Lucio Montanaro ◽  
Fioretta Rambelli
Keyword(s):  
Affinity Chromatography ◽  
Simple Method ◽  
Blue Dextran ◽  
A Chain ◽  
Dye Affinity Chromatography ◽  
Blue Sepharose

A rapid and simple method for the isolation of the two chains of ricin is described. The method involves two chromatographic runs, the first on blue-Sepharose and the second on blue dextran-Sepharose. It is moreover shown that the A chain of ricin, but not the B chain, binds to poly(U)-Sepharose.

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.

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