-transparent.png){kind=logo}
The sequences of two phosphopeptides isolated from the catalytic subunit of bovine cardiac muscle cAMP-dependent protein kinase (type II) and from two of its cyanogen bromide fragments, have been determined. One phosphorylation site is a threonyl residue located approximately 180 residues from the blocked NH2 terminus. Its sequence is: -Gly-Arg-Thr-Trp-Thr(P)-Leu-Cys- and includes one of the three sulfhydryl groups present in the molecule. The second phosphorylated site within the sequence: -Val-Ser(P)-Ile-Asn- is located towards the carboxyl end of the protein where the other 2 cysteinyl residues also reside. The finding that phosphorylation of the catalytic subunit occurs on two discrete sites rather than at random suggests that it might be of physiological importance, e.g. in the regulation of enzyme activity.
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
November 1982,
Biochemistry,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
December 1977,
Biochemistry,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
October 1975,
Biochemistry,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
May 1989,
Journal of biochemical and biophysical methods,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
April 1977,
The Journal of biological chemistry,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
April 1973,
Biochimica et biophysica acta,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
August 1974,
The Journal of biological chemistry,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
July 1976,
Biochemical and biophysical research communications,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
June 1976,
The Journal of biological chemistry,
S Shoji, and
K Titani, and
J G Demaille, and
E H Fischer
May 1979,
Biokhimiia (Moscow, Russia),
