Isolation and partial characterization of distinct species of phosphotyrosyl protein phosphatases from rat spleen.
Three phosphotyrosine protein phosphatases (PTP-I PTP-II and PTP-III) inhibited by Zn2+ and active on the phosphotyrosyl residues included into the acidic co-polymer poly (Glu, Tyr) 4:1 previously phosphorylated by a spleen tyrosyl kinase have been resolved and partially purified from rat spleen cytosol by DEAE cellulose chromatography followed by phosphocellulose chromatography and/or Ultrogel AcA 44 gel filtration. PTP-I (Mr 65,000 by gel filtration) was purified about 1000 folds. It is stimulated by EDTA and unaffected by either vanadate (50 microM) or molybdate (up to 25 microM). PTP-II (Mr 30,000) and PTP-III (Mr 50,000) are insensitive to EDTA and inhibited by molybdate. In addition PTP-III is also inhibited by vanadate.
D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003600:Cytosol / Q000201:enzymology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases; D051381:Rats; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity
D010749:Phosphoprotein Phosphatases; D017027:Protein Tyrosine Phosphatases