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The kinetics of phosphorylation of the Sepharose-coupled peptide RRASVA by catalytic subunit of protein kinase A, and diastereomers of this peptide, containingd-amino acids successively in each position, were studied. Coupling of these peptides with the amino and carboxyl termini to CH- and AH-Sepharoses had similar effects on the phosphorylation reaction, increasing theK m and decreasing...
Rat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated into unphosphorylated and fully phosphorylated enzyme. The effects of fructose 2,6-bisphosphate and AMP on these two enzyme forms were examined. Unphosphorylated fructose-1,6-bisphosphatase was more easily inhibited by both effectors. Fructose 2,6-bisphosphate affected both K 0.5 and V m...
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