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J. Biol. Chem., Vol. 265, Issue 8, 4583-4591, Mar, 1990
JD Pearson, DB DeWald, WR Mathews, NM Mozier, HA Zurcher-Neely, RL Heinrikson, MA Morris, WD McCubbin, JR McDonald and ED Fraser
The complete primary structure has been determined for an inhibitor protein
of protein kinase C. The bovine brain-derived inhibitor has a pI of 6 and
its N-terminal alanine residue is blocked by acetylation. Fragments
obtained by chemical and enzymatic cleavage of the purified inhibitor were
analyzed by Edman degradation, fast atom bombardment mass spectrometry, and
tandem mass spectrometry. The results establish that the protein has a
calculated average molecular mass of 13,690 daltons and contains 125 amino
acid residues with the following sequence: (sequence: see text) The
inhibitor does not show significant homology with any other known protein.
Circular dichroism of the freshly prepared apoprotein indicated a secondary
structural content of 23% alpha-helix, 31% beta-sheet, and 11% beta-turn.
Immobilization on nitrocellulose followed by exposure to a
65Zn2(+)-containing overlay solution showed that, like protein kinase C
itself, the inhibitor is a zinc-binding protein, although the sequence does
not reveal a "zinc finger" structure. Competition with 10-fold molar excess
Ca2+ or Mg2+ did not reduce the zinc-binding specificity of this inhibitor.
Amino acid sequence and characterization of a protein inhibitor of protein kinase C
Department of Biopolymer Chemistry, Upjohn Company, Kalamazoo, Michigan 49001.
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