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0 ml fractions are collected starting with the addition of the sample. The fractions may be analyzed by the Elson-Morgan reaction 2~ (see this volume [3]). It is advisable to partially neutralize the acid in each fraction so as not to use up all the buffer needed for the color reaction. 3 N HC1 should be analyzed at the same time and should similarly be partially neutralized. The amount of glucosamine or galactosamine present in the sample is determined by addition of the amounts present in the fractions belonging to each component.

Bourrillon, R. Got, and D. Meyer, Biochim. Biophys. Acta 83, 178 (1964). [2] CARBOHYDRATE UNITS OF GLYCOPROTEINS 35 4. Gel Filtration. In addition to being useful in separating glycopeptides from non-carbohydrate-containing peptides and amino acids present in proteolytic digests of glycoproteins, gel filtration can be used to separate glycopeptides differing substantially in molecular weight. Since the glyeopeptides originating from one type of carbohydrate unit are likely to be of similar molecular weight, they cannot be resolved by this procedure.

This property makes possible their chromatography on diethylaminoethyl(DEAE)-cellulose columns. It is advisable to carry out this type of chromatography at a pit fairly close to neutrality in order to avoid removing or degrading the sialic acid. The sample should be placed on DEAE-cellulose columns at a very low ionic strength, as it has been found that otherwise complete adsorption of all of the negatively charged material is not obtained. 3,~ Elution can be achieved with a linear gradient. 1 M buffer at the pH to be used, and then with the dilute buffer in which the sample is to be applied.

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