Purification of a regulatory subunit of type II cAMP-dependent protein kinase from Drosophila heads

Hiroko Inoue, Tohru Yoshioka

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    The cytosolic extract from Drosophila heads was separated using anion-exchange column chromatography. Two types of cAMP-dependent protein kinase (PKA), type I and type II, were detected, and type II PKA was found to be a major isozyme. The regulatory subunit of type II PKA (RII) was purified, and only one isoform was observed. The purified protein had an apparent molecular mass of 51 kDa on SDS gel electrophoresis. Partial amino acid sequences of the protein were almost identical with the RIIα subunit of human. Since PKA has been implicated to be especially important for learning and memory in Drosophila, the RII subunit may play an essential role in the regulation of neuronal activity in the brain of Drosophila, and possibly in human.

    Original languageEnglish
    Pages (from-to)223-226
    Number of pages4
    JournalBiochemical and Biophysical Research Communications
    Issue number1
    Publication statusPublished - 1997 Jun 9


    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

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