Activity and specificity of covalently immobolized wheat germ agglutinin toward cell surfaces
1973; Wiley; Volume: 15; Issue: 5 Linguagem: Inglês
10.1002/bit.260150515
ISSN1097-0290
AutoresDane W. Zabriskie, David F. Ollis, Max M. Burger,
Tópico(s)Viral gastroenteritis research and epidemiology
ResumoAbstract 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.
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