Measurement of Hyaluronidase Enzyme Activity in Venom of Iranian Vipera Lebetina

Document Type : Original Article

Authors

1 Msc in Biochemistry.Department of Biochemistry, Faculty of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran.

2 MSC Student of Biochemistry Graduate.Department of Biochemistry, Faculty of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran.

3 Expert Laboratory.Department of Laboratory, Faculty of Medicine, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran.

Abstract

Background and Objective: Snake venoms comprise complex mixtures of enzymatic and non-enzymatic proteins and small organic compounds. Hyaluronidase is a constant factor in the venom of the snake and is known as a spreading factor.  This factor facilitate spread of toxins that harm into the blood circulation system.
In this paper, we describe the determination of hyaluronidase activity in Iranian Vipera lebetina venom.
Subjects and Methods: Hyaluronidase activity was assayed turbidometrically on hyaluronic acid. Turbidity reducing activity was expressed as a percentage of the hydrolysed hyaluronate, taking the absorbance of a tube as 100% in which no enzyme was added. Bovin testis hyaluronidase was used as standard.
Results: The optima PH and temperature for hyaluronidase maximum activity was 6 and 37 °C respectively.
Conclusion: In conclusion the Iranian Vipera lebetina venom possessed considerable hyaluronidase activity.
 

Keywords


1-Girish K, Shashidharamurthy R, Nagaraju S, Gowda TV, Kemparaju K. Isolation and characterization of hyaluronidase a “spreading factor” from Indian cobra (Naja naja) venom. Biochimie 2004;86(3):193-202.
2-Pessini AC, Takao TT, Cavalheiro EC, Vichnewski W, Sampaio SV, Giglio JR, et al. A hyaluronidase from Tityus serrulatus scorpion venom: isolation, characterization and inhibition by flavonoids. Toxicon 2001;39(10):1495-504.
3-Morey SS, Kiran K, Gadag J. Purification and properties of hyaluronidase from Palamneus gravimanus (Indian black scorpion) venom. Toxicon 2006;47(2):188-95.
4-Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J biol Chem 1951;193(1):265-75.
5-Pukrittayakamee S, Warrell DA, Desakorn V, McMichael AJ, White NJ, Bunnag D. The hyaluronidase activities of some Southeast Asian snake venoms. Toxicon 1988;26(7):629-37.
6-El-Safory NS, Fazary AE, Lee C-K. Hyaluronidases, a group of glycosidases: Current and future perspectives. Carbohydrate Polymers 2010;81(2):165-81.
7-Girish K, Kemparaju K. Inhibition of Naja naja venom hyaluronidase: role in the management of poisonous bite. Life sciences 2006;78(13):1433-40.
8-Stern R, Asari AA, Sugahara KN. Hyaluronan fragments: an information-rich system. European journal of cell biology 2006;85(8):699-715.
9-Zhong D, Meng Q, Li J, Wang Y, Zhang X, Wang S, et al. A hyaluronidase from the snake venom of Agkistrodon blomhoffii ussurensis of Changbai mountain: isolation and characterization. International Journal of Biology 2010;2(2):p171.
10-Janardhan P, Rosenblum D, Strichartz RS. Numerical experiments in Fourier asymptotics of Cantor measures and wavelets. Experimental Mathematics 1992;1(4):249-73.
11-Harrison RA, Ibison F, Wilbraham D, Wagstaff SC. Identification of cDNAs encoding viper venom hyaluronidases: cross-generic sequence conservation of full-length and unusually short variant transcripts. Gene 2007;392(1):22-33.