The -amylase of the Beetle Callosobruchus chinensis. Properties.

@article{Podoler1971TheO,
  title={The -amylase of the Beetle Callosobruchus chinensis. Properties.},
  author={H Podoler and Shalom W. Applebaum},
  journal={The Biochemical journal},
  year={1971},
  volume={121 2},
  pages={321-5}
}
C. chinensis larval amylase is activated by Ca(2+) and inhibited by Cl(-) and EDTA (K(i) 6.7x10(-3)m). GSH and 2-mercaptoethanol activate, presumably at different sites, as 2-mercaptoethanol interferes with Ca(2+) activation, whereas GSH enhances it. The inhibition by iodoacetic acid and N-ethylmaleimide (K(i) 1.55x10(-2)m) suggest that free thiol groups are essential for activity. The pH optimum of 5.2-5.4 is moved to 5.6-5.8 by Ca(2+) and 2-mercaptoethanol. The activation energy is 7270 cal… CONTINUE READING

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