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Structural characterization and biosynthesis of gp87, a melanoma‐associated oncofetal antigen defined by monoclonal antibody 140.240
Author(s) -
Khosravi Mohammed J.,
Dent Peter B.,
Liao ShuenKuei
Publication year - 1985
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910350112
Subject(s) - oncofetal antigen , neuraminidase , epitope , monoclonal antibody , antigen , glycoprotein , tunicamycin , sialic acid , antibody , microbiology and biotechnology , chemistry , glycopeptide , biochemistry , biology , immunology , tumor associated antigen , gene , enzyme , unfolded protein response , antibiotics
Abstract The monocolnal antibody 140.240, which reacts with a melanoma‐associated oncofetal antigen, identifies an epitope present on an 87 kd molecule present on the surface of melanoma cells. This molecule is a singlechain monomer, which by tunicamycin treatment and two‐dimensional tryptic mapping has been shown to arise from a 77 kd polypeptide precursor (p77). This precursor is rapidly glycosylated to an 83 kd intermediate (gp83) which in turn is rapidly further glycosylated into the mature 87 kd glycopolypeptie (gp87). Neuraminidase treatment of the glycopeptides indicates that only gp87 contains accessible sialic acid moieties.