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Arch Insect Biochem Physiol. 2002 Jan;49(1):56-64.

Purification and characterization of protein phosphatase-1 from two cold-hardy goldenrod gall insects.

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Institute of Biochemistry and Department of Chemistry, Carleton University, Ottawa, Ontario, Canada.


The catalytic subunit of protein phosphatase-1 (PP-1) was purified to homogeneity from final instar larvae (the overwintering stage) of freeze avoiding (Epiblema scudderiana) and freeze tolerant (Eurosta solidaginis) cold-hardy insects. Arrhenius plots showed that activity of PP-1 from both species was strongly suppressed at low temperature. Acidic shifts in pH optima and increased inhibition by okadaic acid were also observed when the enzymes were assayed at 4 degrees C compared with 24 degrees C. The data identify multiple ways by which PP-1 can be inhibited at low temperature and this inhibition appears to be key to sustaining high glycogen phosphorylase activity in support of polyol synthesis at low temperatures.

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