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- W1538178082 abstract "Publisher Summary This chapter describes methods to induce specific modifications of cysteine-rich regions in the regulatory and catalytic domains of Protein Kinase C (PKC) by oxidant tumor promoters and PKC-specific inhibitors involving oxidations or alkylating mechanisms. These procedures have been standardized using α, β and γ isoenzymes of PKC, and the discussion is limited to these isoenzymes. Oxidatively modified proteins exhibit increased susceptibility to proteolysis compared to native proteins. If trace amounts of proteases are present in the preparations of enzyme used for oxidative modification experiments, even though oxidative activation of the enzyme might have occurred, it may not be noticed as the modified enzyme may be rapidly degraded, resulting in an apparent inactivation of enzyme. Because calpain proteolytically activates PKC and prefers oxidatively modified proteins, it is important to remove any contaminating calpain from the purified preparations of PKC. Calpain-derived PKC (M-kinase) that contains only the catalytic domain can be employed to study selective modification of cysteine residues in this domain. Because PKC is purified and stored in the presence of thiol agents, it is important to remove the agents from the PKC preparation prior to enzyme modification studies." @default.
- W1538178082 created "2016-06-24" @default.
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- W1538178082 date "1995-01-01" @default.
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- W1538178082 title "[14] Modifications of cysteine-rich regions in protein kinase C induced by oxidant tumor promoters and enzyme-specific inhibitors" @default.
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- W1538178082 doi "https://doi.org/10.1016/0076-6879(95)52016-3" @default.
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