Protein analysis of NCA-50 shows identity to NCA cDNA deduced sequences and indicates posttranslational modifications.
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 phosphatidyl-inositol glycan, via an amide linkage to ethanolamine at amino acid position 287, which has replaced the last 24 amino acids.
Grunert
F
F
Institute for Immunobiology, University of Freiburg, FRG.
Kolbinger
F
F
Schwarz
K
K
Schwaibold
H
H
von Kleist
S
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D001483:Base Sequence; D001943:Breast Neoplasms / Q000473:pathology; D015815:Cell Adhesion Molecules; D004247:DNA / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis* / Q000235:genetics; D006031:Glycosylation; D006801:Humans; D008113:Liver Neoplasms / Q000032:analysis / Q000556:secondary; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000032:analysis*
D000596:Amino Acids; D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D015815:Cell Adhesion Molecules; D006023:Glycoproteins; D011506:Proteins; D004247:DNA