Affinity isoelectric focusing in polyacrylamide gel--a method to detect ligand-binding proteins.

[1]  V. Hořejší Review: Affinity electrophoresis. , 1981, Analytical biochemistry.

[2]  J. Novotný,et al.  Studies on lectins. XLVII. Some properties of D-galactose binding lectins isolated from the seeds of Butea frondosa, Erythrina indica and Momordica charantia. , 1980, Biochimica et biophysica acta.

[3]  K. Takeo,et al.  Determination of dissociation constants by affinity electrophoresis: Complexes between human serum proteins and concanavalin A , 1980 .

[4]  V. Hořejší Some theoretical aspects of affinity electrophoresis , 1979 .

[5]  M. Tichá,et al.  Studies on lectins. XLIV. The pH dependence of lectin interactions with sugars as determined by affinity electrophoresis. , 1979, Biochimica et biophysica acta.

[6]  V. Hořejší,et al.  Studies on lectins. XXXV. Water-soluble O-glycosyl polyacrylamide derivatives for specific precipitation of lectins. , 1978, Biochimica et biophysica acta.

[7]  V. Hořejší,et al.  Studies on lectins. XXXVI. Properties of some lectins prepared by affinity chromatography on O-glycosyl polyacrylamide gels. , 1978, Biochimica et biophysica acta.

[8]  M. Tichá,et al.  Studies on lectins. XXXII. Application of affinity electrophoresis to the study of the interaction of lectins and their derivatives with sugars. , 1977, Biochimica et biophysica acta.

[9]  M. Tichá,et al.  Studies on lectins. XXXI. Determination of dissociation constants of lectin. Sugar complexes by means of affinity electrophoresis. , 1977, Biochimica et biophysica acta.

[10]  K. Takeo,et al.  Dissociation constants of glucan phosphorylases of rabbit tissues studied by polyacrylamide gel disc electrophoresis. , 1972, Archives of biochemistry and biophysics.

[11]  P. Righetti,et al.  Isoelectric focusing in polyacrylamide gels. , 1971, Biochimica et biophysica acta.

[12]  G. Entlicher,et al.  Studies on phytohemagglutinins III. Isolation and characterization of hemagglutinins from the pea (Pisum sativum L.) , 1970 .