Proteolytic profile of Vipera ammodytes snake venom

Acta Veterinaria

Volumn 50, Issue 5-6, 2000, Pages 345-354

  Kristina, Gopčević ^a   Ivanka, Karadžić ^a   Lidija, Izrael ^a   Mirjana, Pavlović ^a   Vucetic J ^b  

^a UNIVERSITY OF BELGRADE   (Serbia)

^b UNIVERSITY OF BELGRADE   (Serbia)

Author keywords

Inhibition; Proteases; Snake venom

Indexed keywords

AMMODYTES; FUNGI; SERPENTES; VIPERA AMMODYTES;

EID: 0346355831     PISSN: 05678315     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (19)

1. Bradford MM, 1976; A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem, 72, 248-254.
2. Catanese JJ and Cress LF, 1985; Enzymatic digestion of human plasma inter-alpha-trypsin inhibiitor by snake venom metalloproteinases. Comp Biochem Physiol, 80 B, 507-512.
3. Cvetković M, Petković D, and Zdjelar K, 1988; Inhibition of proteolytic enzymes by heparin. Yugoslav Physiol Pharmacol Acta, 24 . 53-54.
4. Cvetković M, Petković D, Pavlović M, Zdjelar K, Bosnić O, Mujović V, 1990; Inhibition of proteolytic enzymes by prostacyclin (PGI2). 7th International Conference on prostaglandins and related Compounds, Florence, p 364.
5. Gutierrez JM, Romero M, Diaz C, Borkow G, Ovadia M, 1995; Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper. Toxicon 33, 19-29.
6. Hashimoto Y, Tsuiki S, Nishizawa K, Pigman W, 1963; Action of proteolytic enzymes on purified bovine submaxillary mucin. Ann NY Acad Sci, 105, 233-246
7. Iwanaga S. and Suzuki T, 1979; Enzymes in snake venoms. In: Handbook of Experimental Pharmacology, 2, 61 (Chen-Yuan Lee, Ed.) Springer-Verlag, Berlin.
8. Kress L and Catanese JJ, 1981; Effects of human plasma alpha-2-macroglobulin on the proteolytic activity of snake venom. Toxicon 19, 227-228.
9. Labib R Z, Awad ERž Farag NW, 1981; Proteases of Cerastes cerastes (Egyptian sand viper) and Cerastes vipera (Sahara sand viper) snake venoms. Toxicon 19, 227-228.
10. Mićević D, 1989; Proučavanje bioloških efakata frakcija otrova viperida in vivo i in vitro. Doktorska disertacija, Medicinski fakultet, Beograd.
11. Muić N, Plantanida M, 1955; Zur Kentniss des Sandottergites Electrophoretische und chemische characterisierung der Hauptfractionen. Z Phys Chem. 299, 6-12.
12. Petković D, Pavlović M, Jovanović T, Panić-Držajić V, Zdjelar K, Unković S, et al, 1988; Neutralization of Vipera ammodytes ammodytes snake venom by the antitoxinum viperinum and calcihept. lugoslav Physiol Pharmacol Acta, 24, Suppl 6, 343-344.
13. Petković D, Pavlović M, Jovanović T, Panić-Držajić V, Zdjelar K, Unković S, et al, 1991; Neutralization of the activity of Vipera ammodytes ammodytes snake venom on myocardium of rats by antitoxinum viperinum - a histopathological study. J Tox Clin Exp, 11 (6), 343-347.
14. Pfleiderer G, Celliers P, Stanulović M, Wachsmuth ED, Determann H, Braunitzer G, 1964; Properties and analytical application of the kidney-particle aminopeptidase. Biochem J, 340, 552-564.
15. Ritonja A. and Gubenšek F, 1985; Ammodytoxin A, a highly lethal phospholipase A2 from Vipera ammodytes ammodytes venom. Bioch Biophys Acta, 828, 306-312.
16. Stepanov VM, Rudenskaya GN, Nestereva NG, Kupriyanova TI, Khokhlova Yu M, Usaite laet al, 1980; Serinovaya proteinaza Thermoactinomyces vulgaris INMI 4a. Biokhimiya 45, 1871-1880.
17. Stiles BG, Sexton FW and Weinstein SA, 1991; Antibacterial effects of different snake venoms -purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake). Toxicon 29, 1129-1141.
18. Vanden Berghie DA, Vlietnick A.J, 1991; Screening methods for antibacterial and antiviral agents from higher plants. In Methods in Plants Biochemistry; Hostettman, K., Ed.; Academic Press; London, Chapter 3, pp 47-60.
19. Zdjelar K, Macut D, Cvetković M, Petković D, 1990; The proteolytic effects of Vipera ammodytes snake venom in the presence of heparin and hyaluronic acid. Toxicon 28 (2), p 169.