Amino acid sequence of a 12-kDa inhibitor of protein kinase C |
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Authors: | N M Mozier H A Zürcher-Neely D M Guido W R Mathews R L Heinrikson E D Fraser M P Walsh J D Pearson |
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Affiliation: | Biochemistry Department, Upjohn Laboratories, Kalamazoo, MI 49001. |
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Abstract: | 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. |
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