A hydroxyproline-containing glycopeptide released from the walls of sycamore tissue-culture cells by hydrazinolysis.
Degradation of the sycamore cell wall by hydrazinolysis yielded soluble glycopeptides. The peptide portion of the predominant glycopeptide was shown to be cyclic (4-trans-hydroxy-l-prolyl)-4-trans-hydroxy- l-proline. From this structure and the composition of the major glycopeptide it was deduced that only short oligosaccharides are attached to the hydroxyprolyl residues of the wall glycoprotein. Detailed evidence for the structure of the peptide is given in a supplementary paper that has been deposited as Supplementary Publication SUP 50020, at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.
D001089:Arabinose / Q000032:analysis; D002250:Carbon Radioisotopes; D002473:Cell Wall / Q000032:analysis*; D002849:Chromatography, Gas; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D046508:Culture Techniques; D004590:Electrophoresis, Paper; D006020:Glycopeptides / Q000032:analysis*; D006834:Hydrazines; D006909:Hydroxyproline / Q000032:analysis*; D013058:Mass Spectrometry; D011392:Proline / Q000032:analysis; D013055:Spectrophotometry, Infrared; D014197:Trees; D014316:Tritium
D002250:Carbon Radioisotopes; D006020:Glycopeptides; D006834:Hydrazines; D014316:Tritium; D011392:Proline; D001089:Arabinose; D006909:Hydroxyproline