Purification and characterization of chymotrypsins isolated from the midgut of two cyclorrhaphan larvae [electronic resource].

By: Description: p.1-9Uniform titles:
  • Efflatoun's Journal of Entomology, 2009 v.9 [electronic resource].
Subject(s): Online resources: In: Efflatoun's Journal of Entomology 2009.v.9Summary: The larval midgut CTLPs of the two cyclorrhaphans Parasarcophaga hertipes and Musca crassirostris were purified. They have an approximate molecular weight range of 21-25 KDa and have subunits linked with disulphide covalent bonds. Activity of both enzymes has alkaline pH optima in the pH range 8-9. The purified enzymes showed considerable stability in media of acidic pHs and at high temperature, and they do not need metal ions for their activation. The purified CTLPs were inhibited at different degrees by PMSF, TPCK, chymostatin, and SBI. The presented data are discussed.
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The larval midgut CTLPs of the two cyclorrhaphans Parasarcophaga hertipes and Musca crassirostris were purified. They have an approximate molecular weight range of 21-25 KDa and have subunits linked with disulphide covalent bonds. Activity of both enzymes has alkaline pH optima in the pH range 8-9. The purified enzymes showed considerable stability in media of acidic pHs and at high temperature, and they do not need metal ions for their activation. The purified CTLPs were inhibited at different degrees by PMSF, TPCK, chymostatin, and SBI. The presented data are discussed.

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