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

Hiroko Inoue, Tohru Yoshioka

    Research output: Contribution to journalArticle

    7 Citations (Scopus)

    Abstract

    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
    Volume235
    Issue number1
    DOIs
    Publication statusPublished - 1997 Jun 9

    Fingerprint

    Cyclic AMP-Dependent Protein Kinases
    Protein Kinases
    Drosophila
    Purification
    Head
    Column chromatography
    Molecular mass
    Electrophoresis
    Isoenzymes
    Anions
    Chromatography
    Amino Acid Sequence
    Brain
    Protein Isoforms
    Proteins
    Gels
    Learning
    Data storage equipment
    Amino Acids

    ASJC Scopus subject areas

    • Biochemistry
    • Biophysics
    • Molecular Biology

    Cite this

    Purification of a regulatory subunit of type II cAMP-dependent protein kinase from Drosophila heads. / Inoue, Hiroko; Yoshioka, Tohru.

    In: Biochemical and Biophysical Research Communications, Vol. 235, No. 1, 09.06.1997, p. 223-226.

    Research output: Contribution to journalArticle

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