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Activity and specificity of covalently immobolized wheat germ agglutinin toward cell surfaces
Author(s) -
Zabriskie Dane,
Ollis David F.,
Burger Max M.
Publication year - 1973
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260150515
Subject(s) - covalent bond , wheat germ agglutinin , wheat germ , biochemistry , chemistry , covalent binding , polyacrylamide , germ , agglutinin , enzyme , polyacrylamide gel electrophoresis , microbiology and biotechnology , biology , lectin , organic chemistry
Wheat germ agglutinin protein, which is able to agglutinate tumor cells better than normal cells, was covalently bound to polyacrylamide gel beads. The specific binding activity of the protein was preserved on these beads and was expressed heterogeneously by the binding of mouse leukemia cells (L1210) to the protein coupled gels. The selective activity of the immobilized protein was maximal when the number of sites available to covalently couple the protein was lowest. The application of this observation to the general field of covalent immobilization of proteins and enzymes may be of considerable utility.