1979
DOI: 10.1042/bst0070781
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Glycoproteins: a Tribute to Albert Neuberger A Joint Colloquium of the Carbohydrate Groups of the Biochemical Society and the Chemical Society

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“…Better results were obtained with an affinity adsorbent prepared by amidating CH-Sepharose with D-galactosamine [5]. At pH 8, even in 2 M NaCl, the lectin is adsorbed completely, whereas at pH 5 about two-thirds leaves the column, the residual activity is eluted on raising the NaCl concentration to 2 M. 1 ml of the affinity gel retains more than 3 mg of the purified lectin.…”
Section: Resultsmentioning
confidence: 99%
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“…Better results were obtained with an affinity adsorbent prepared by amidating CH-Sepharose with D-galactosamine [5]. At pH 8, even in 2 M NaCl, the lectin is adsorbed completely, whereas at pH 5 about two-thirds leaves the column, the residual activity is eluted on raising the NaCl concentration to 2 M. 1 ml of the affinity gel retains more than 3 mg of the purified lectin.…”
Section: Resultsmentioning
confidence: 99%
“…Affinity adsorbents were prepared either by coupling p-aminophen yl N-acetyl-fi-D-galactosdminide to cyanogen-bromide-activated Sepharose 4 B [4J or by amidation of CH-Sepharose with an amino sugar using the water-soluble l-ethyl-3-(3-dimethylamino-propy1)-carbodiimide as a condensing agent [5].…”
Section: Methodsmentioning
confidence: 99%