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Inhibition of protein phosphorylation by chloroquine

Archives of Microbiology, 1987
The rapid phase of fructose-1,6-bisphosphatase (FBPase) inactivation following glucose addition to starved yeast cells [reported previously] is inhibited on addition of 10 mM chloroquine (CQ) at about pH 8. This inhibition of inactivation was shown to be due to the prevention of phosphorylation of the enzyme.
H, Kalisz, G, Pohlig, H, Holzer
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Phosphorylation of Proteins by Inositol Pyrophosphates

Science, 2004
The inositol pyrophosphates IP 7 and IP 8 contain highly energetic pyrophosphate bonds. Although implicated in various biologic functions, their molecular sites of action have not been clarified. Using radiolabeled IP 7
Adolfo, Saiardi   +4 more
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Phosphorylation of Microtubule‐Associated Proteins

European Journal of Biochemistry, 1976
1. Tubulin is not an adenosine-3':5'-monophosphate-dependent (cyclic-AMP-dependent) protein kinase. Both entities have been clearly separated by sucrose gradient ultracentrifugation. With a tubulin preparation obtained by the polymerization-depolymerization technique protein kinase had a sedimentation coefficient of 8.7 S whereas tubulin sedimented ...
L, Rappaport   +4 more
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Protein Phosphorylation

Annual Review of Biochemistry, 1975
C S, Rubin, O M, Rosen
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Opioid Peptides and Protein Phosphorylation

1979
The identification and isolation of naturally occur ring neuropeptides with morDhine-like activity was first reported by Hughes (1975) and co-workers (HUGHES, et al, 1975). These compounds were named methionine-enkephalin and leucine-enkephalin and have the amino-acid sequences of Tyr-Gly-Gly-Phe-Met and Tyr-Gly-Gly-Phe-Leu, respectively. Subsequently,
L G, Davis, Y H, Ehrlich
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Analysis of Phosphorylation of Unlabeled Proteins

Current Protocols in Molecular Biology, 1997
AbstractPhosphorylation of unlabeled proteins can be detected using immunological or enzymatic techniques. Anti‐phosphotyrosine antibodies are used with immunoblots to detect tyrosine phosphorylation. This unit provides a protocol for detection of antibodies by 125I‐labeled protein A or enhanced chemiluminescence (ECL).
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Protein phosphorylation and the respiratory burst

Archives of Biochemistry and Biophysics, 1988
The exposure of 32P-loaded neutrophils to any of a variety of activating agents induces changes in the levels of phosphorylation of a large number of phosphoproteins. The uptake of phosphate by one set of phosphoproteins in particular, a family whose members migrate at Mr 48K with near neutral pI values, appears to be closely related to the activation ...
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Participation of annexins in protein phosphorylation

Cellular and Molecular Life Sciences (CMLS), 1997
Simultaneous discovery of members of the annexin family of calcium and phospholipid binding proteins by several groups is intimately linked to the possibility that these proteins may be controlled by phosphorylation. Indeed, annexin I and annexin II have been identified as major substrates for the tyrosine kinase activity associated with epidermal ...
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Protein Phosphorylation

1999
Abstract Reversible phosphorylation is one of the major mechanisms of controlling protein activity in all eukaryotic cells. This new edition of Protein Phosphorylation: A Practical Approach provides a comprehensive description of current methods used to study protein phosphorylation and the kinases and phosphatases which catalyse it ...
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Protein Phosphorylation

1993
Abstract Reversible phosphorylation is one of the major mechanisms by which protein activity is controlled in all eukaryotic cells. Networks of protein kinases and phosphatases, which catalyse phosphorylation and dephosphorylation respectively, are responsible for switching between different pathways of cell division, development, or ...
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