The availability of a VG 70-250SE high-mass range mass spectrometer will make possible the detailed chemical study of a number of glycoproteins and peptides related to cancer biology and cell biology. The structures of N-linked saccharides present in lysosomal membrane glycoproteins, lysosomal enzymes, in the congenital anemia HEMPAS and sulfated N-glycans will be investigated. These studies will provide the structural information on molecular signals for targeting of lysosomal components to lysosome and cell surface, identifying glycosyltransferases defective in HEMPAS, and elucidate a new type of sulfated saccharides which may be abundant in tumor cells. The structure of O-linked saccharides present in human lymphoid cells and meconium will be investigated. These studies will provide carbohydrate differentiation markers, some of which may be shared by tumor cells. In addition, the identification and quantitation of various N- and O-acyl derivatives of sialic acid will be investigated as oncodevelopmental markers. The chemical structure of proteins and peptides with adhesive functions will be investigated. The derivatives of active fragment, RGD, will be synthesized and tested for its adhesive activity. The various peptides including cyclic will be identified by FAB-MS. The proteins made by recombinant technology will be analyzed to elucidate disulfide bond structures and to confirm the peptide sequence by FAB-MS.
