The subcellular location at which hydroxylysine residues of collagen are glycosylated was studied in chick embryo fibroblasts. Ribosomes were isolated from 14C-lysine pulse-labeled cells in tissue culture. Alkaline hydrolysis followed by amino acid analysis and scintillation counting of the effluent showed that glucosylgalactosyl hydroxylysine and galactosyl hydroxylysine as well as hydroxylysine and lysine were the major 14C-labeled components. Acid hydrolysis destroyed the glycoconjugates and yielded only free 14C-hydroxylysine and 14C-lysine. These data indicate that glycosylation of peptide-bound hydroxylysine is initiated while the polypeptide chain is still in the stages of assembly on the ribosome.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Mar 17 1975|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology