Polyamines and basic proteins stimulate activation by cAMP and catalytic activity Mucor rouxii

Marcelo Guthmann, Ricardo Pastori, Silvia Moreno

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

Partial activation of Mucor rouxii cAMP-dependent protein kinase by cAMP was obtained when kemptide was used as substrate, but complete activation was attained with cAMP plus protamine or histone. Full activation could not be achieved by increasing kemptide or cAMP concentration. Complete activation by cAMP could be obtained by addition of 10 μM polylysine, 10 μM lysine-rich histone or 0.5 mM spermine plus spermidine. The degree of stimulation could be up to 5-fold, depending on the amount of enzyme in the assay. The same concentrations of polycations increased 1.5-2.3-fold the Vmax of kemptide phosphorylation by the free catalytic subunits of both Mucor and bovine heart protein kinases; 10 μM polyarginine inhibited completely the activity of both enzymes.

Original languageEnglish (US)
Pages (from-to)395-402
Number of pages8
JournalCellular Signalling
Volume2
Issue number4
DOIs
StatePublished - 1990
Externally publishedYes

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Keywords

  • cAMP-dependent
  • Mucor rouxii
  • Polyamines
  • Polycations
  • Protein kinase

ASJC Scopus subject areas

  • Cell Biology

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