Tonks, N. K., Diltz, C. D., Fischer, E. H. (1991) Purification of protein-tyrosine phosphatases from human placenta. Methods in Enzymology, 201. pp. 427-442. ISSN 0076-6879
Abstract
This chapter discusses the purification of protein-tyrosine phosphatases from human placenta. Phosphorylation of proteins on tyrosyl residues is an essential element in the control of normal and neoplastic cell growth. The phosphorylation state of a protein reflects the relative activities of the kinase that phosphorylates it and the phosphatase that removes the phosphate. A major technical difficulty associated with the study of protein phosphatases is the requirement for suitably purified phosphorylated substrates. Characterization of the protein-tyrosine phosphatases (PTPases) provides a necessary complementary perspective for an overall understanding of the control of cellular function by tyrosine phosphorylation. This chapter describes procedures for the preparation of substrates and assay of PTPases. It also discusses the purification of a major low-molecular-weight PTPase from human placenta.
| Item Type: | Paper |
|---|---|
| Uncontrolled Keywords: | XENOPUS OOCYTES CLONING FAMILY DEPHOSPHORYLATION MICROINJECTION EXPRESSION MUSCLE KIDNEY CD45 CDNA |
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase |
| CSHL Authors: | |
| Communities: | CSHL labs > Tonks lab |
| Depositing User: | Matt Covey |
| Date: | 1991 |
| Date Deposited: | 17 Dec 2013 15:32 |
| Last Modified: | 17 Dec 2013 15:32 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/29089 |
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