Abstract
Gel filtration on Sephadex G-25 permits a rapid and relatively mild isolation of serum mucoproteins, directly from deproteinized perchloric acid filtrates of blood sera, even without previous concentration and neutralisation. During the elution mucoproteins (fraction I) separate from a fraction of glycopolypeptide character (fraction II) and from a third, easily dialysable fraction of peptides (fraction III). The peak of the deproteinizing agents and of low-molecular Folin-Ciocalteu-positive substances coincides with the peak of polypeptides (fraction II). The isolated mucoproteins of fraction I can be separated by paper electrophoresis at pH 8.6 to give two sub-fractions; on Sephadex G-200 at least two subfractions are also detectable. By the method described it is possible to perform a fractional separation of mucoproteins with a small amount of serum.
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