Partial purification and characterization of phosphotyrosyl-protein phosphatase(S) from human erythrocyte cytosol

Phosphotyrosyl-protein phosphatase activity of human erythrocyte cytosol can be resolved into two fractions by DEAE-cellulose chromatography followed by P-cellulose chromatography. Both 32P-Tyr-phosphatases are able to dephosphorylate 32P-Tyr of poly (Glu-Tyr) 4:1 but not angiotensin II and syntheti...

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Published inBiochemical and biophysical research communications Vol. 137; no. 1; pp. 566 - 572
Main Authors Clari, Giulio, Brunati, Anna Maria, Moret, Vittorio
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 29.05.1986
Elsevier
Subjects
4-Nitrophenylphosphatase - blood
Applied sciences
Chromatography, DEAE-Cellulose
Erythrocytes - enzymology
Exact sciences and technology
Humans
Other techniques and industries
Phosphoprotein Phosphatases - blood
Phosphotyrosine
Substrate Specificity
Tyrosine - analogs & derivatives
Tyrosine - metabolism
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Abstract Phosphotyrosyl-protein phosphatase activity of human erythrocyte cytosol can be resolved into two fractions by DEAE-cellulose chromatography followed by P-cellulose chromatography. Both 32P-Tyr-phosphatases are able to dephosphorylate 32P-Tyr of poly (Glu-Tyr) 4:1 but not angiotensin II and synthetic peptide Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Arg-Gly, previously phosphorylated on tyrosine residues by rat spleen tyrosine-protein kinase. Both 32P-Tyr-phosphatase activities distinctly differ from either 32P-Tyr-phosphatase activity or “acid” and “alkaline” p-nitrophenylphosphatase activities with regard to catalytic and physico-chemical properties such as substrate specificity, chromatographic behaviour, response to various effectors.
AbstractList Phosphotyrosyl-protein phosphatase activity of human erythrocyte cytosol can be resolved into two fractions by DEAE-cellulose chromatography followed by P-cellulose chromatography. Both 32P-Tyr-phosphatases are able to dephosphorylate 32P-Tyr of poly (Glu-Tyr) 4:1 but not angiotensin II and synthetic peptide Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Arg-Gly, previously phosphorylated on tyrosine residues by rat spleen tyrosine-protein kinase. Both 32P-Tyr-phosphatase activities distinctly differ from either 32P-Ser-casein phosphatase activity or "acid" and "alkaline" p-nitrophenylphosphatase activities with regard to catalytic and physico-chemical properties such as substrate specificity, chromatographic behaviour, response to various effectors.
Phosphotyrosyl-protein phosphatase activity of human erythrocyte cytosol can be resolved into two fractions by DEAE-cellulose chromatography followed by P-cellulose chromatography. Both 32P-Tyr-phosphatases are able to dephosphorylate 32P-Tyr of poly (Glu-Tyr) 4:1 but not angiotensin II and synthetic peptide Asp-Ala-Glu-Tyr-Ala-Ala-Arg-Arg-Gly, previously phosphorylated on tyrosine residues by rat spleen tyrosine-protein kinase. Both 32P-Tyr-phosphatase activities distinctly differ from either 32P-Tyr-phosphatase activity or “acid” and “alkaline” p-nitrophenylphosphatase activities with regard to catalytic and physico-chemical properties such as substrate specificity, chromatographic behaviour, response to various effectors.
Author Brunati, Anna Maria
Moret, Vittorio
Clari, Giulio
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Snippet Phosphotyrosyl-protein phosphatase activity of human erythrocyte cytosol can be resolved into two fractions by DEAE-cellulose chromatography followed by...
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SubjectTerms 4-Nitrophenylphosphatase - blood
Applied sciences
Chromatography, DEAE-Cellulose
Erythrocytes - enzymology
Exact sciences and technology
Humans
Other techniques and industries
Phosphoprotein Phosphatases - blood
Phosphotyrosine
Substrate Specificity
Tyrosine - analogs & derivatives
Tyrosine - metabolism
Title Partial purification and characterization of phosphotyrosyl-protein phosphatase(S) from human erythrocyte cytosol
URI https://dx.doi.org/10.1016/0006-291X(86)91248-9
https://www.ncbi.nlm.nih.gov/pubmed/2424449
https://search.proquest.com/docview/76889528
Volume 137
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