Protein analysis of NCA-50 shows identity to NCA cDNA deduced sequences and indicates posttranslational modifications

• Published in: Biochemical and biophysical research communications Vol. 153; no. 3; pp. 1105 - 1115
• Main Authors: Grunert, F., Kolbinger, F., Schwarz, K., Schwaibold, H., von Kleist, S.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 30.06.1988
• Subjects: Amino Acid Sequence; Amino Acids - analysis; Antibodies, Monoclonal; Antigens, Neoplasm; Base Sequence; Breast Neoplasms - pathology; Cell Adhesion Molecules; DNA - analysis; Glycoproteins - analysis; Glycoproteins - genetics; Glycosylation; Humans; Liver Neoplasms - analysis; Liver Neoplasms - secondary; Molecular Sequence Data; Protein Conformation; Protein Processing, Post-Translational; Proteins - analysis; glcN; SDS-PAGE; DTE; DTNB; PTH; FAB-MS; TFMSA; EA; NCA; CEA; MAb; PCA
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(88)81342-1

The amino acid sequence, representing 59% of the protein moiety of NCA-50 (nonspecific crossreacting antigen), has been determined. These data confirm that NCA-50 is the product of the mRNA whose corresponding cDNAs were recently isolated from a human lung (HLC-1), as well as from a colon carcinoma cell line (SW 403) cDNA library. The four cysteine residues detected in the NCA-50 molecule form disulfide bonds. The glycosylation of 7 potential N-glycosylation sites which were analysed, showed pronounced differences. There is strong evidence that NCA-50 is bound to a phosphatidylinositol glycan, via an amide linkage to ethanolamine at amino acid position 287, which has replaced the last 24 amino acids.