Abstract

N-Myristoyl transferase (NMT) is the enzyme that covalently modifies several proteins important in signal transduction. Streptozotocin-induced diabetes resulted in a 2-fold increase in NMT activity from rat liver as compared to control animals. Administration of sodium orthovanadate to the diabetic rats reduced the activity of the NMT to 75–120% of the control values. Elevated NMT activity was observed with both cAMP-dependent protein kinase-derived and pp60 src-derived peptide substrates. No significant change in the apparent K m was observed with the cAMP-dependent protein kinase-derived peptide substrate. Unlike in rat brain, in all conditions highest NMT activity was observed in the fraction of rat liver.

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