Abstract
The radioactive products derived from transfer of [ 14C]mannose residues from GDP-[ 14C]mannose to endogenous acceptors of a Hansenula holstii particulate enzyme preparation have been solubilized by Pronase digestion. From this soluble mixture, glycopeptides containing [ 14C]mannose have been purified and have been shown by β-elimination-reduction experiments to contain radioactive mannose and oligosaccharides of mannose linked to serine and threonine residues. Radioactive macromolecular complexes of mannan-protein were extracted from the particulate enzyme fraction with hot, neutral citrate buffer. These components contained variable quantities of protein, mannose, and phosphate. The more neutral components were reduced in size by Pronase digestion and yielded glycopeptides similar to those obtained by direct Pronase digestion of the particulate fraction.
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