Amino acid sequence at the phosphorylated site of rat liver fructose-1,6-diphosphatase and phosphorylation of a corresponding synthetic peptide
- 29 October 1979
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 90 (3), 1064-1072
- https://doi.org/10.1016/0006-291x(79)91934-x
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- In vivo and in vitro phosphorylation of rat liver fructose-1,6-bisphosphatase.Proceedings of the National Academy of Sciences, 1977
- Primary structure of the S-peptide formed by digestion of rabbit liver fructose 1,6-bisphosphatase with subtilisinArchives of Biochemistry and Biophysics, 1977
- Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.Journal of Biological Chemistry, 1977
- Purification and characterization of catalytic subunit of skeletal muscle adenosine 3':5'-monophosphate-dependent protein kinase.Journal of Biological Chemistry, 1977
- The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liverBiochemical and Biophysical Research Communications, 1976
- Synthetic substrate for cyclic AMP-dependent protein kinaseNature, 1975
- A method for measuring the Čerenkov radiation produced by 32P in small sample volumesAnalytical Biochemistry, 1975
- Peptides from myelin basic protein as substrates for adenosine 3′, 5′-cyclic monophosphate-dependent protein kinasesBiochemical and Biophysical Research Communications, 1974
- Rapid reciprocal changes of rat hepatic glycolytic enzymes and fructose-1,6-diphosphatase following glucagon and insulin injection in vivoBiochemical and Biophysical Research Communications, 1972
- Strategy and tactics in protein chemistryBiochemical Journal, 1970