The specific purification of various carbohydrate-binding hemagglutinins

The specific affinity adsorbent prepared by cross-linking the inhibitory sugar of the hemagglutinin to be purified to insoluble starch with epichlorhydrin was applied to the purification of various carbohydrate-binding hemagglutinins. The hemagglutinin can be isolated in essentially one step, and th...

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Published inBiochemical and biophysical research communications Vol. 46; no. 5; pp. 1810 - 1815
Main Authors Matsumoto, Isamu, Osawa, Toshiaki
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 10.03.1972
Subjects
Acetates
Animals
Antibodies - isolation & purification
Chemical Phenomena
Chemistry
Chromatography, Affinity
Cyanogen Bromide
Eels
Ethers, Cyclic
Fucose
Galactosamine
Glycoproteins
Lectins - isolation & purification
Oligosaccharides
plants
Polysaccharides
Starch
Thyroglobulin
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Summary:The specific affinity adsorbent prepared by cross-linking the inhibitory sugar of the hemagglutinin to be purified to insoluble starch with epichlorhydrin was applied to the purification of various carbohydrate-binding hemagglutinins. The hemagglutinin can be isolated in essentially one step, and the adsorbent can be used several times with little changes in its capacity. If the effective inhibitory substance for the hemagglutinin is glycoprotein, the adsorbent prepared by coupling the glycoprotein to activated Sepharose is recommended for the purification of the hemagglutinin.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(72)90055-1