Purification of protein-tyrosine phosphatases from human placenta

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

URL: http://www.ncbi.nlm.nih.gov/pubmed/1719346
DOI: 10.1016/0076-6879(91)01039-5

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: http://repository.cshl.edu/id/eprint/29089

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