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Preparation and isolation of immunologically active glycopeptides from carcinoembryonic antigen (CEA)
Author(s) -
Banjo C.,
Gold P.,
Gehrke C. W.,
Freedman S. O.,
Krupey J.
Publication year - 1974
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.2910130202
Subject(s) - carcinoembryonic antigen , glycopeptide , chemistry , glycoprotein , biochemistry , glutamine , antigen , radioimmunoassay , asparagine , chromatography , aspartic acid , enzyme , amino acid , microbiology and biotechnology , biology , immunology , genetics , cancer , antibiotics
In order to determine the structure of the tumor‐specific immunodominant group of the carcinoembryonic antigen (CEA) of human gastro‐intestinal tumors, immunologically active fragments from this glycoprotein were prepared by partial enzymatic hydrolysis using the proteolytic enzyme nagase. The fragments were purified by sequential molecular sieve, adsorption and ion exchange chromatography, and were analysed for carbohydrate and amino‐acid composition by gas‐liquid chromatography. The antigenic activity of each fragment was tested using both the Z‐gel and Farr radioimmunoassay techniques for CEA. Immunologically active glycopeptides with molecular weights of 1,000–5,000 Daltons, which contained the tumor antigenic determinant of CEA, had relatively high contents of N‐acetyl‐D‐glucosamine, aspartic acid or asparagine, and glutamic acid or glutamine.