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J. Winzler, J. Biol. Chem. 238, 21 (1963). • R. G. Spiro and M. J. Spiro, J. Biol. Chem. 240, 997 (1965). J R. G. Spiro, J. Biol. Chem. 242, 1915 (1967). o j. T. Cassidy, G. W. Jourdian, and S. Roseman, J. Biol. Chem. 240, 3501 (1965). h R. C. Hughes and R. W. Jeanloz, Biochemistry 3, 1535 (1964). R. G. Spiro, J. Biol. Chem. 242, 4813 (1967). i R. Kornfeld, J. Keller, J. Baenziger, and S. Kornfeld, J. Biol. Chem. 246, 3259 (1971). k R. Kornfeld and S. Kornfeld, J. Biol. Chem. 245, 2536 (1970). z R.

For example, incubation of thyroglobulin glycopeptides containing the mannoseN-acetylglucosamine unit with a jack bean q-mannosidase preparation which had some fl-N-acetylglucosaminidase activity indicated that all the mannose residues were released before one N-acetylglucosamine residue was liberated indicating the internal location of the latter sugar -~'~ (Fig. 6). The release of sialic acid and N-acetylhexosamines can be followed colorimetrically by performing the thiobarbituric acid reaction (Vol.

Biochem. 6 5 , 191 (1969). 2O [1] THE CARBOHYDRATES OF GL¥COPROTEINS 21 their linkages to more internal sugars, these enzymes can split 0-glycosidic glycopeptide bonds, such as the N-acetylgalactosaminyl-serine (threonine), galactosyl-hydroxylysine, and xylosyl-serine linkages. Generally the enzymes act optimally on glycopeptides where steric hindrances imposed by the peptide chain of the whole glycoprotein are not present. Modification of the glycopeptides may be necessary to permit enzymatic action, such as the N-acetylation of hydroxylysine which is required for the splitting of the galactosylhydroxylysine bondf-2 Release of a sugar can sometimes be effected by an enzyme of given specificity from one source but not from another.

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