Boerner, R J <br/><br/>
Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity.  [electronic resource] 

 -  Biochemistry  Nov 1995 
 - 15351-8 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi00046a044  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Binding Sites<br/>Calcium--pharmacology<br/>Catalysis<br/>Chromatography, High Pressure Liquid<br/>Disulfides--metabolism<br/>Edetic Acid--pharmacology<br/>Enzyme Inhibitors--pharmacology<br/>Humans<br/>Isoelectric Focusing<br/>Kinetics<br/>Magnesium--pharmacology<br/>Magnetic Resonance Spectroscopy<br/>Mass Spectrometry<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>Peptide Fragments--metabolism<br/>Phosphoric Monoester Hydrolases--antagonists & inhibitors<br/>Phosphorylation<br/>Proto-Oncogene Proteins pp60(c-src)--chemistry<br/>Recombinant Proteins--metabolism