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Estimating glycoprotein carbohydrate chain structures by lectin reactivities in polyacrylamide gels
Author(s) -
Nicolson G. L.,
Irimura T.
Publication year - 1984
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/j.1768-322x.1984.tb00294.x
Subject(s) - glycoprotein , carbohydrate , lectin , biochemistry , biology , polyacrylamide gel electrophoresis , gel electrophoresis , sodium dodecyl sulfate , electrophoresis , glycosylation , polyacrylamide , microbiology and biotechnology , enzyme
Complex mixtures of cellular glycoproteins contain a myriad of different carbohydrate chains that cannot be easily analyzed without rigorous purification of each individual glycoprotein. We have analyzed the carbohydrate chains in complex mixtures of cellular glycoproteins by separation using sodium dodecyl‐sulfate polyacrylamide gel electrophoresis and interacting the gels with several 125I‐labeled lectins. By use of in situ chemical modifications of the glycoproteins after their electrophoretic separation together with the known carbohydrate‐binding specifities of several lectins, it has been possible to estimate glycoprotein carbohydrate chain structures. As an example we have examined the cellular glycoproteins of a ovary‐colonizing metastatic variant of B16 melanoma and report the types of carbohydrate chains that are found on various melanoma glycoproteins.