Purification of the catalytically active phosphorylated form of insulin receptor kinase by affinity chromatography with O-phosphotyrosyl-binding antibodies
- 1 October 1985
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 242 (1), 176-186
- https://doi.org/10.1016/0003-9861(85)90491-6
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Relationship between the subunit structure of insulin receptor and its competence to bind insulin and undergo phosphorylationArchives of Biochemistry and Biophysics, 1984
- Artifacts associated with 2-mercaptoethanol upon high resolution two-dimensional electrophoresisAnalytical Biochemistry, 1984
- The .beta. subunit of the insulin receptor kinase is an insulin-activated proteinBiochemistry, 1983
- A dot-immunobinding assay for monoclonal and other antibodiesAnalytical Biochemistry, 1982
- Phosphotyrosine-containing proteins isolated by affinity chromatography with antibodies to a synthetic haptenNature, 1981
- Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivityAnalytical Biochemistry, 1981
- Purification and properties of insulin receptors from rat liver membranesBiochemical and Biophysical Research Communications, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- A simplified method for cyanogen bromide activation of agarose for affinity chromatographyAnalytical Biochemistry, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970