Study of Protease Properties in Pseudocereastes Percicus Venom

Document Type : Full Research Paper

Authors

1 Proteomics and Biochemistry Department, Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization (AREEO), Karaj, Iran

2 Department of Microbiology, School of Specialized Science, Science and Research Branch, Islamic Azad University, Tehran, Iran

Abstract

Snakes are one of the most useful animals in the world for the production of medicines, sera and vaccines that are made from the venom. Venomous snakes have many therapeutic applications and are very useful in biochemical research. Snake venom is an oily liquid, white to yellow with a slightly acidic pH and is a complex mixture of polypeptides, toxic proteins, enzymes, pharmaceuticals and non-protein substances. Venom of all snakes is not the same, although it is believed that venom of snakes originated from common biological ancestors.
The aim of this study was to determine the activity of protease enzyme in venom of horned snake from different regions. In this study, the venom of the horned snake from three regions of Semnan, Kerman and Khuzestan was investigated. At first, the venom protein concentration of this snake was determined using Lowry and Bradford methods, which was reported to be 950 mg / ml (95%). In the next step, the number of peptides and molecular weight of these proteins were determined by vertical electrophoresis, which were performed in both reducing and non-reducing methods. And the molecular weight range of 15 to 190 kDa was estimated to have relative similarities in Khuzestan, Kerman and Semnan. Native electrophoresis and casein substrate electrophoresis confirmed the proteolytic activity of ruminant venom and quantitative determination of venom proteolytic activity was determined by BAPNA dilution and casein digestion
11.56 U/ml.

Keywords

References

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Veterinary Research & Biological Products
Volume 33, Issue 1
March 2020
Pages 118-127

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History

  • Receive Date: 05 October 2019
  • Revise Date: 13 January 2020
  • Accept Date: 17 February 2020

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