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. 1972 Oct;129(5):995–1002. doi: 10.1042/bj1290995a

Histone phosphatase and cyclic nucleotide-stimulated protein kinase from human lymphocytes

A W Murray 1, M Froscio 1, B E Kemp 1
PMCID: PMC1174257  PMID: 4348170

Abstract

1. Extracts of human peripheral blood lymphocytes contained a histone phosphatase that catalysed the release of Pi from phosphorylated whole thymus histone. 2. Stimulation of the phosphatase was obtained by concentrations of KCl and NaCl of up to 75mm, and by MgCl2; CaCl2 inhibited the enzymic activity. 3. In the absence of MgCl2, phosphoenol-pyruvate inhibited histone phosphatase activity; this inhibition could be partially reversed by adding MgCl2 to assays. 4. Lymphocyte extracts contained a protein kinase activity which was maximally stimulated by 1μm-cyclic AMP (adenosine 3′:5′-cyclic monophosphate) or by 0.1mm-cyclic GMP (guanosine 3′:5′-cyclic monophosphate). 5. Incubation of the enzyme with histone in the absence of ATP or MgCl2 resulted in the dissociation of the enzyme into a lower-molecular-weight species that was not stimulated by cyclic AMP. This effect could be prevented if ATP and MgCl2 were present in reaction mixtures before histone and enzyme were allowed to interact. 6. Cyclic AMP also dissociated the kinase into a lower-molecular-weight species. 7. In the presence of 1μm-AMP, half-maximal activities were obtained with 0.92mm-MgCl2, 6.0μm-ATP and 0.23mg of whole thymus histone/ml.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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