scholarly journals Physicochemical and Biological Characterization of Fucoidan from Fucus vesiculosus Purified by Dye Affinity Chromatography

Marine Drugs ◽  
2016 ◽  
Vol 14 (4) ◽  
pp. 79 ◽  
Author(s):  
Ahmed Zayed ◽  
Kai Muffler ◽  
Thomas Hahn ◽  
Steffen Rupp ◽  
Doris Finkelmeier ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Fucus Vesiculosus ◽  
Biological Characterization ◽  
Dye Affinity Chromatography

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.

The Immunological Characterization of Human Antibodies to Factor VIII Isolated by Immuno-Affinity Chromatography

1981 ◽  
Vol 45 (01) ◽  
pp. 060-064 ◽  
Author(s):  
M L Kavanagh ◽  
C N Wood ◽  
J F Davidson
Keyword(s):  
Factor Viii ◽  
Affinity Chromatography ◽  
Gel Filtration ◽  
Immunological Characterization ◽  
Human Antibodies ◽  
Heavy Chains ◽  
Light Chain Type ◽  
Antibody Preparations ◽  
Chain Type

SummaryNine human antibodies to factor VIII were isolated from haemophilic plasmas by affinity chromatography and gel filtration and six were subsequently subjected to immunological characterization. Three partially purified preparations were similarly characterized. Eight of the antibodies were characterized as being exclusively IgG and one preparation was found to contain IgM. Seven of the antibodies contained only a single light chain type, four being of type lambda and three of type kappa. Two antibody preparations contained both kappa and lambda light chains. In four of the preparations, only a single heavy chain sub-class could be demonstrated, three of IgG3 and one of IgG4. Of the remainder, three were a mixture of IgG3 and IgG4 sub-classes and one contained both IgG2 and IgG4. IgG sub-classification could not be achieved with the IgM-containing preparation. These results demonstrate a restricted heterogeneity of light and heavy chains in human antibodies to factor VIII.

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