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J. Biol. Chem., Vol. 262, Issue 16, 7613-7617, Jun, 1987
AR Bengur, EA Robinson, E Appella and JR Sellers
We have determined the sequence of the sites phosphorylated by protein
kinase C in the turkey gizzard smooth muscle myosin light chain. In
contrast to previous work (Nishikawa, M., Hidaka, H., and Adelstein, R. S.
(1983) J. Biol. Chem. 258, 14069-14072), two-dimensional tryptic peptide
maps of both heavy meromyosin and the isolated myosin light chain showed
two major phosphopeptides, one containing phosphoserine and the other
phosphothreonine. We have purified the succinylated tryptic phosphopeptides
using reverse phase and DEAE high pressure liquid chromatography. The
serine-containing peptide, residues 1-4 (Ac- SSKR), is the NH2-terminal
peptide. The phosphorylated serine residue may be either serine 1 or serine
2. The threonine-containing peptide, residues 5-16, yielded the sequence
AKAKTTKKRPQR. Analysis of the yields and radioactivity of the products from
automated Edman degradation showed that threonine 9 is the phosphorylation
site.
Sequence of the sites phosphorylated by protein kinase C in the smooth muscle myosin light chain
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