1. Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom.
- Author
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Yonamine CM, Kondo MY, Juliano MA, Icimoto MY, Baptista GR, Yamane T, Oliveira V, Juliano L, Lapa AJ, Lima-Landman MT, and Hayashi MA
- Subjects
- Amino Acid Sequence, Animals, Arginine chemistry, Arginine metabolism, Binding Sites, Biocatalysis drug effects, Circular Dichroism, Crotalid Venoms chemistry, Crotalid Venoms metabolism, Dose-Response Relationship, Drug, Hydrogen-Ion Concentration, Hydrolysis, Kinetics, Molecular Sequence Data, Neurotoxins chemistry, Neurotoxins metabolism, Peptides chemistry, Peptides metabolism, Serine Proteases chemistry, Sodium Chloride pharmacology, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Substrate Specificity, Temperature, Crotalid Venoms enzymology, Crotalus metabolism, Serine Proteases metabolism
- Abstract
This work describes for the first time the characterization of the enzymatic features of gyroxin, a serine protease from Crotalus durissus terrificus venom, capable to induce barrel rotation syndrome in rodents. Measuring the hydrolysis of the substrate ZFR-MCA, the optimal pH for proteolytic cleavage of gyroxin was found to be at pH 8.4. Increases in the hydrolytic activity were observed at temperatures from 25 °C to 45 °C, and increases of NaCl concentration up to 1 M led to activity decreases. The preference of gyroxin for Arg residues at the substrate P1 position was also demonstrated. Taken together, this work describes the characterization of substrate specificity of gyroxin, as well as the effects of salt and pH on its enzymatic activity., (Copyright © 2012 Elsevier Masson SAS. All rights reserved.)
- Published
- 2012
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