Open AccessGlycopeptides from Surface Membranes of Neuroblastoma Cells
Author(s) -
Mary Catherine Glick,
Yosef Kimhi,
Uriel Z. Littauer
Publication year - 1973
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.70.6.1682
Subject(s) - trypsinization , glycopeptide , pronase , trypsin , sephadex , cell , neuroblastoma , membrane , chemistry , biology , microbiology and biotechnology , biochemistry , chromatography , cell culture , enzyme , genetics , antibiotics
Sequential removal of surface glycopeptides was achieved by subjection of mouse neuroblastoma cells to a two-step trypsin treatment under different conditions. The glycopetides released by each trypsinization step were digested by Pronase and examined on columns of Sephadex G-50. Different chromatographic patterns were found for the two digests. Thus, several groups of glycopeptides can be distinguished by the trypsinization procedure. One group is readily removed and appears to be at a more accessible location on the cell surface. Among the four neuroblastoma clones examined, the glycopeptide patterns from axon-forming cells differed from those of axon-minus cells.