Avtor/Urednik		Zrimšek, P; Kos, J; Gubenšek, F
Naslov		Immunological detection of pharmacologically active sites on toxins from Vipera ammodytes ammodytes venom
Tip		članek
Vir		In: Cestnik V, Pogačnik A, editors. Referati 6. Zavrnikovega spominskega sestanka; 1995 nov 9-11; Lipica. Ljubljana: Veterinarska fakulteta,
Leto izdaje		1997
Obseg		str. 151-4
Jezik		eng
Abstrakt		Ammodytin L is a myotoxic phospholipase AZ homologue from the European viper Vipera ammodytes ammodytes venom with low phospholipatic or neurotoxic activity. Polyclonal antibodies were used for the determination of myotoxic site on ammodytin L. Possible antigenic sites were predicted on the basis of the primary structure of ammodytin L, tertiary structure of its homologue PLA2 from the American rattle-snake Crotalus atrox and of previous studies of PLA2 myotoxicity. Seven synthetic peptides, corresponding to the possible antigenic sites, were used for the immunization of rabbits. For determination of the titer of specific antibodies against peptides and native antigen, indirect enzyme - linked immunosorbent assay (ELISA) was used. The same method was used also for the determination of relative binding affinity of antipeptide antibodies to ammodytin L and to ammoditoxins A and C. Antibody to M5-KLH exhibited the highest binding affinity to ammodytin L, whereas antibody to M3-alb mainly bound ammodytoxins A and C. Lethality determination of ammodytin L complexes with antipeptide antibodies has shown that anti-M1-KLH antibody efficiently protected experimental animals indicating the association of M 1 region on ammodytin L molecule with myotoxic activity.
Deskriptorji		VIPER VENOMS RABBITS MICE ENZYME-LINKED IMMUNOSORBENT ASSAY VIPERIDAE