Purification and characterization of a soluble catalytic fragment of the human transmembrane leukocyte antigen related (LAR) protein tyrosine phosphatase from an Escherichia coli expression system.
摘要：
A 350 amino acid soluble fragment of the catalytic domain of the () protein tyrosine has been purified 17-fold to greater than 90% purity from an expression vector in quantities sufficient for kinetic and structural characterization. To assess substrate specificity, phosphotyrosine corresponding to sites of the two major classes of tyrosine kinases have been synthesized. Thus 6-12-residue phosphotyrosine of the and kinase domains and of the and C-terminal regulatory sites of and p56lck have been analyzed for kcat and KM by using a nonradioactive chromogenic assay for release. The catalytic domain of shows kcat values of 20-70 s-1 for phosphotyrosine and affinities that vary 150-fold from 27 microM to 4.1 mM.
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DOI：
10.1021/bi00239a019
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年份：
1991
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