Amino acid sequence of a 12-kDa inhibitor of protein kinase C.
The complete primary structure of a bovine-brain-derived inhibitor of protein kinase C has been established. Fragments of the purified protein were obtained by cleavage with cyanogen bromide, Staphylococcus aureus V8 protease, trypsin and chymotrypsin. Subsequent analysis of the resulting fragments by fast-atom-bombardment mass spectrometry and Edman degradation revealed a calculated molecular mass of 11,779 Da with the following 107-amino-acid sequence: [sequence: see text] This inhibitor does not share significant primary structural identity with any other known protein.
Mozier
N M
NM
Biochemistry Department, Upjohn Laboratories, Kalamazoo, MI 49001.
Zürcher-Neely
H A
HA
Guido
D M
DM
Mathews
W R
WR
Heinrikson
R L
RL
Fraser
E D
ED
Walsh
M P
MP
Pearson
J D
JD
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology; D002417:Cattle; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D004791:Enzyme Inhibitors / Q000737:chemistry*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011493:Protein Kinase C / Q000037:antagonists & inhibitors*; D014357:Trypsin
D004791:Enzyme Inhibitors; D010446:Peptide Fragments; D011493:Protein Kinase C; D002918:Chymotrypsin; D014357:Trypsin; D003488:Cyanogen Bromide