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- W2071750282 abstract "The effect of tautomycin (TM) on protein kinase C (PKC) was studied in a cell-free system. TM, like phorbol dibutyrate (PDBu), enhanced both base-line and Ca2+/phospholipids-dependent protein kinase activity. However, PDBu but not TM increased the affinity of the enzyme for calcium ions (Ca2+), suggesting that TM is a new activator of PKC, distinct from PDBu. In the presence of 10 micrograms/ml phosphatidyl inositol, the activity of PKC reached maximum at 10(-3) M Ca2+ concentration when the other co-factors were absent. Both TM and PDBu increased the maximum level of PKC activity at the optimum concentration of Ca2+, suggesting that they interacted with the site of PKC which is distinct from the site where Ca2+ interacts. TM and PDBu did not activate the enzyme when protamine sulfate in place of histone III-S was used as a substrate, indicating that they activate PKC by affecting the regulatory domain of the enzyme." @default.
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- W2071750282 date "1989-01-01" @default.
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- W2071750282 title "Comparison of the effect of tautomycin and phorbol ester on protein kinase C in a cell-free system." @default.
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- W2071750282 doi "https://doi.org/10.7164/antibiotics.42.1290" @default.
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