Yeast cyclic AMP‐dependent protein kinase
- 29 October 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 163 (1) , 28-32
- https://doi.org/10.1016/0014-5793(83)81155-7
Abstract
We have purified cyclic AMP-dependent protein kinase from the yeast Saccharomyces cerevisiae. The purified enzyme was inactive in the absence of cyclic AMP and displayed two protein bands on SDS gel electrophoresis. One was identified as the cAMP-binding protein by chromatography on cAMP-agarose. M r of the latter was 50 000 while the catalytic subunit had an M r of 59 000. The enzyme accepted yeast phosphorylase, glycogen synthase and fructose 1,6-bisphosphatase as substrates. No inhibition by the mammalian protein kinase inhibitor was observed.Keywords
This publication has 13 references indexed in Scilit:
- Characterization of phosphorylase kinase activities in yeastBiochemical and Biophysical Research Communications, 1983
- Characterization of phosphoprotein phosphatases and phosphorylase phosphatase from yeastBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Cyclic nucleotide‐dependent inactivation of yeast fructose 1,6‐bisphosphatase by ATPFEBS Letters, 1982
- Isolation and Properties of Two Protein Kinases from Yeast which Phosphorylate Casein and Some Ribosomal ProteinsEuropean Journal of Biochemistry, 1978
- Purification and properties of a yeast protein kinaseBiochemistry, 1975
- Proteins and Sodium Dodecyl Sulfate: Molecular Weight Determination on Polyacrylamide Gels and Related ProceduresPublished by Elsevier ,1975
- Cyclic 3′,5′-adenosine monophosphate stimulates trehalose degradation in baker's yeastBiochemical and Biophysical Research Communications, 1974
- Analysis of bacteriophage T7 early RNAs and proteins on slab gelsJournal of Molecular Biology, 1973
- Affinity chromatography of phosphofructokinase using Cibacron blue F3G-AJournal of Chromatography A, 1972
- Purification and properties of yeast glycogen phosphorylase a and bBiochemistry, 1971