PMID: 8594416Jul 19, 1995Paper

Purification and characterization of multiple S6 phosphatases from the rat parotid gland

Molecular and Cellular Biochemistry
N Yokoyama

Abstract

S6 phosphatase activities, which dephosphorylate the phosphorylated S6 synthetic peptide, RRLSSLRASTSKSESSQK, were purified to near homogeneity from the membrane and cytosolic fractions of the rat parotid gland. Multiple S6 phosphatases were fractionated on Mono Q and gel filtration columns. In the cytosolic fraction, at least three forms of S6 phosphatase, termed peaks I, II, and III, were differentially resolved. The three forms had different sizes and protein compositions. The peak I enzyme, which had an approximately Mr of 68 kDa on gel filtration, appears to represent a dimeric form of the 39 kDa protein. This S6 phosphatase showed the high activity in the presence of EGTA and was completely inhibited by nanomolar concentrations of either okadaic acid or inhibitor 2. The peak II S6 phosphatase enzyme, with an Mr of 35 kDa, was activated by Mn2+. This form could be a proteolytic product of the catalytic subunit of type 1 phosphatase, due to its sensitivities to okadaic acid and inhibitor 2. The peak III enzyme, with an Mr of 55 kDa, is a Mn(2+)-dependent S6 phosphatase. This S6 phosphatase can be classified as a type 1 phosphatase, due to its sensitivity to okadaic acid, since the IC50 of okadaic acid is 4 nM. However, the ...Continue Reading

References

Jul 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·A R OlivierG Thomas
Jan 1, 1988·Methods in Enzymology·D L Brautigan, C L Shriner
Feb 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·E Erikson, J L Maller
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Oct 1, 1983·The Journal of Cell Biology·F S GorelickJ D Jamieson
Apr 1, 1982·European Journal of Biochemistry·R Duncan, E H McConkey

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Citations

Jul 7, 2001·Journal of Interferon & Cytokine Research : the Official Journal of the International Society for Interferon and Cytokine Research·N YokoyamaW T Miller

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