Active site labeling of a receptor-like protein tyrosine phosphatase

The inactivation of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase (PTPase), by iodoacetate and not by iodoacetamide suggested that iodoacetate interacts in a highly selective manner with the enzyme. The data indicate that iodoacetate binds at the active site of the...

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Veröffentlicht in:	The Journal of biological chemistry 1992-01, Vol.267 (1), p.140-143
Hauptverfasser:	Pot, D A, Dixon, J E
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Aniline Compounds - pharmacology Animals Binding Sites Binding, Competitive Biological and medical sciences Chromatography, High Pressure Liquid Enzyme Activation - drug effects Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glycoproteins - antagonists & inhibitors Glycoproteins - metabolism Hydrolases Iodoacetates - pharmacology Iodoacetic Acid LAR protein Molecular Sequence Data Organophosphorus Compounds - pharmacology Protein Tyrosine Phosphatases - antagonists & inhibitors Protein Tyrosine Phosphatases - genetics Protein Tyrosine Phosphatases - metabolism protein-tyrosine phosphatase Rats Receptor-Like Protein Tyrosine Phosphatases, Class 4 Receptors, Cell Surface Recombinant Proteins - antagonists & inhibitors Recombinant Proteins - genetics Recombinant Proteins - metabolism
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