Purification, characterization and cDNA sequence of an alkaline chymotrypsin from the midgut of Manduca sexta.

@article{Peterson1995PurificationCA,
  title={Purification, characterization and cDNA sequence of an alkaline chymotrypsin from the midgut of Manduca sexta.},
  author={Allison M. Peterson and Gonzalez-Herrera Fernando and Michael A. Wells},
  journal={Insect biochemistry and molecular biology},
  year={1995},
  volume={25 7},
  pages={
          765-74
        }
}
The chymotrypsin in the midgut of Manduca sexta has been purified, characterized and the cDNA encoding the protein has been cloned. The enzyme exists as a monomer of approx. 24 kDa and shows maximal activity between pH 10.5 and 11.0. Kinetic studies reveal that the Michaelis constant (Km) for the synthetic substrate N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide varies only slightly between pH 7.5 and 11.5 and the Dixon plot shows a kinetically significant pKa at 9.2. The specificity of the purified… CONTINUE READING

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