Abstract
Hydroxyproline-poor glycoprotein contains a single polypeptide chain with lysine at the N-terminus. Removal of carbohydrate attached to serine by alkali treatment produces two polypeptide fractions. Labeling with 35S indicates that most serine residues having a carbohydrate substituent removed by alkali occur on the polypeptide fraction of lower molecular weight. Following alkali treatment, two additional N-terminal amino acids, proline and glycine, were detected suggesting that alkali treatment also cleaves peptide bonds. Methylation analysis of native and degraded glycoproteins, extracted 24, 27, and 36 hours after wounding, demonstrates the following structural features of carbohydrate attached to serine. Arabinose may be (1 → 2)-, (1 → 3)-, or (1 → 5)-linked, glucose occurs as a chain of β-(1 → 4)-linked residues, and galactose occurs as a nonreducing terminal unit.
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Selected References
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