English Journal

Ammodytagin, a heterodimeric metalloproteinase from Vipera ammodytes ammodytes venom with strong hemorrhagic activity.

Kurtović T, Brgles M, Leonardi A, Balija ML, Križaj I, Allmaier G, Marchetti-Deschmann M, Halassy B.SourceResearch and Development Department, Institute of Immunology, Inc, Rockefellerova 10, 10 000 Zagreb, Croatia. tkurtovic@imz.hr
Toxicon : official journal of the International Society on Toxinology.Toxicon.2011 Nov;58(6-7):570-82. Epub 2011 Sep 14.
Ammodytagin, a hemorrhagic Zn(2+)-dependent metalloproteinase from Vipera ammodytes ammodytes (Vaa) venom, is a glycosylated heterodimer of 108 kDa, as determined by MALDI mass spectrometry. Partial amino acid sequencing by Edman degradation and MS/MS analysis identified sequences belonging to metal
PMID 21933678

Purification and biochemical characterization of a novel hemorrhagic metalloproteinase from horned viper (Cerastes cerastes) venom.

Boukhalfa-Abib H, Meksem A, Laraba-Djebari F.SourceLaboratoire de Biologie Cellulaire et Moléculaire, Faculté des Sciences Biologiques, Université des Sciences et de Technologie Houari Boumédienne Bab Ezzouar, Alger, Algeria.
Comparative biochemistry and physiology. Toxicology & pharmacology : CBP.Comp Biochem Physiol C Toxicol Pharmacol.2009 Aug;150(2):285-90. Epub 2009 May 24.
Snake venoms contain metalloproteinases that contribute to the local effects observed after envenoming. In this study, a hemorrhagic metalloproteinase (CcH1) was purified from Cerastes cerastes venom by a combination of gel filtration, ion exchange, affinity and RP-HPLC chromatography. The hemorrhag
PMID 19470410