Partial characterization of protein kinase C from an insect cell line

Jyothi Gupta, Roger G.H. Downer

Research output: Contribution to journalArticlepeer-review


The characteristics of protein kinase C (EC from an insect cell line (Choristoneura fumiferana) have been described. DEAE-cellulose chromatography produced a major peak of activity which eluded at 0.04-0.055 M NaCl. The enzyme was sensitive to phosphatidylserine in the presence of calcium. Phorbol 12-myristate 13-acetate (PMA) in nanomolar concentrations stimulated protein kinase C activity 8-fold over basal levels and reduced the enzymes requirement for Ca2+. The enzyme had a Ka of 10 nM for PMA. Diacylglycerols tested included diolein, dilinolein, diarachidonin, oleoyl-acetyl-glycerol, dioctonoyl-sn-glycerol, dipalmitin and distearin. A 2.5- to 3-fold activation was obtained in the presence of 26 μM diolein, 40 μM oleoyl-acetyl-glycerol and 46 μM dioctonoyl-sn-glycerol. The enzyme activity was sensitive to the inhibitor H-7 and 50% inhibition was achieved at a concentration of 52 μM H-7. Phosphatidylinositol enhanced enzyme activity in the absence of phosphatidylserine but phosphatidylethanolamine had no effect.

Original languageEnglish (US)
Pages (from-to)210-214
Number of pages5
JournalBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Issue number2
StatePublished - Dec 8 1993
Externally publishedYes


  • (C. fumiferana)
  • Diacylglycerol
  • H-7
  • Insect cell line
  • Phorbol ester
  • Phospholipid
  • Protein kinase C

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Molecular Biology


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