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Updated: Aug 7, 2026
06:09
Assaying the Kinase Activity of LRRK2 in vitro
Published on: January 18, 2012
Absence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro
Biochemical and Biophysical Research Communications
|July 16, 1986
Abstract:
Cellular retinol-binding protein, cellular retinoic acid-binding protein, and fetal cellular retinol-binding protein were purified to homogeneity and each polypeptide had a molecular weight of 16,000. Their apoproteins were not phosphorylated under the same conditions. Their holoproteins did not inhibit the phosphorylation of histone III-S by protein kinase C. Each of these observations is contrary to the results reported by Cope et al. (Biochem. Biophys. Res. Commun., 120, 593-601, 1984).
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During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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