Purification and characterization of a high-Mr proteinase inhibitor of pro-phenol oxidase activation from crayfish plasma.

@article{Hergenhahn1987PurificationAC,
  title={Purification and characterization of a high-Mr proteinase inhibitor of pro-phenol oxidase activation from crayfish plasma.},
  author={H G Hergenhahn and Anna Asp{\'a}n and Kenneth S{\"o}derh{\"a}ll},
  journal={The Biochemical journal},
  year={1987},
  volume={248 1},
  pages={223-8}
}
Crayfish plasma was found to contain a proteinase inhibitor, which was purified to apparent homogeneity by acid precipitation, affinity chromatography on concanavalin A-Sepharose and hydrophobic-interaction chromatography. The inhibitor is a monomeric protein with an Mr of about 155,000 and a pI in the range 4.6-4.8. It is heat-stable and tolerant to low pH. It inhibits the serine proteinases trypsin and chymotrypsin, but not thrombin or subtilisin. Furthermore, it is efficient in decreasing… CONTINUE READING