Thin-layer chromatography can resolve phosphotyrosine, phosphoserine, and phosphothreonine in a protein hydrolyzate
- 1 February 1989
- journal article
- research article
- Published by Elsevier in Analytical Biochemistry
- Vol. 177 (1) , 138-143
- https://doi.org/10.1016/0003-2697(89)90028-6
Abstract
No abstract availableThis publication has 18 references indexed in Scilit:
- An Mr 180000 protein is an endogenous substrate for the insulin-receptor-associated tyrosine kinase in human placentaBiochemical Journal, 1987
- Separate domains of the insulin receptor contain sites of autophosphorylation and tyrosine kinase activityBiochemistry, 1987
- Purification of the catalytically active phosphorylated form of insulin receptor kinase by affinity chromatography with O-phosphotyrosyl-binding antibodiesArchives of Biochemistry and Biophysics, 1985
- Relationship between the subunit structure of insulin receptor and its competence to bind insulin and undergo phosphorylationArchives of Biochemistry and Biophysics, 1984
- Phosphorylation of Insulin Receptors Solubilized from Rat Skeletal MuscleDiabetes, 1984
- Characterization and use of monoclonal antibodies for isolation of phosphotyrosyl proteins from retrovirus-transformed cells and growth factor-stimulated cells.Molecular and Cellular Biology, 1983
- Phosphotyrosine-containing proteins isolated by affinity chromatography with antibodies to a synthetic haptenNature, 1981
- Changes in protein phosphorylation in Rous sarcoma virus-transformed chicken embryo cells.Molecular and Cellular Biology, 1981
- Phosphorylation-Dephosphorylation of EnzymesAnnual Review of Biochemistry, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970