Bovine inositol monophosphatase: proteolysis and structural studies

  • Greasley P
  • Gore M
  • Rees-Milton K
 et al. 
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Abstract

Bovine brain inositol monophosphatase is inactivated when trypsin catalyses the cleavage of a single peptide bond between Lys-36 and Ser-37. This proteolysis is closely followed by cleavage at two other sites in the protein between Lys-78 and Ser-79 and between Lys-156 and Ser-157 suggesting that all of these sites are exposed in the native conformation of the protein. All of these residues are predicted to lie at the ends of α helices. The most susceptible bond (Lys-36-Ser-37) is predicted to lie in a highly flexible region of the protein. Circular dichroism studies suggest that approximately 40% of the secondary structure of this protein is helical which is similar to that predicted by the algorithm of Gamier et al. [(1978) J. Mol. Biol. 120, 97-120]. © 1993.

Author-supplied keywords

  • Circular dichroism
  • Inositol monophosphatase
  • Protein structure
  • Proteolysis

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Authors

  • P. J. Greasley

  • M. G. Gore

  • K. J. Rees-Milton

  • C. I. Ragan

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