Purification to homogeneity and partial characterization of a 56,000-dalton protein phosphatase from rabbit reticulocytes.
A 56,000-Da peptide with inherent protein phosphatase activity was isolated from the postribosomal supernatant fraction of rabbit reticulocytes. The peptide appears to form complexes with other proteins that are present in crude fractions. It exhibits atypical retention on steric exclusion columns during high performance liquid chromatography, an unusual characteristic that facilitated its isolation. The protein phosphatase activity of the 56,000-Da peptide is dependent on Mn2+ ions, but is not activated by either the FA, ATP/Mg2+ protein phosphatase activator system or by proteolysis. The protein phosphatase activity of the peptide is increased 3-fold or more by the antigen peptides described in the accompanying paper (Fullilove, S., Wollny, E., Stearns, G., Chen, S.C., Kramer, G., and Hardesty, B. (1984) J. Biol. Chem. 259, 2493-2500).
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D007525:Isoelectric Focusing; D007700:Kinetics; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D010749:Phosphoprotein Phosphatases / Q000097:blood* / Q000302:isolation & purification; D010761:Phosphorus Radioisotopes; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D014357:Trypsin / Q000494:pharmacology
D000596:Amino Acids; D010761:Phosphorus Radioisotopes; D008345:Manganese; D010749:Phosphoprotein Phosphatases; D014357:Trypsin