Results 191 to 200 of about 34,979 (216)
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BJ46a, a snake venom metalloproteinase inhibitor

European Journal of Biochemistry, 2001
Fractionation of the serum of the venomous snake Bothrops jararaca with (NH4)2SO4, followed by phenyl‐Sepharose and C4‐reversed phase chromatographies, resulted in the isolation of the anti‐hemorrhagic factor BJ46a. BJ46a is a potent inhibitor of the SVMPs atrolysin C (class P‐I) and jararhagin (P‐III) proteolytic activities and B.
R H, Valente   +4 more
openaire   +2 more sources

Snake Venom Metalloproteinases

2021
Charlotte A. Dawson   +3 more
openaire   +1 more source

Synthetic and endogenous inhibitors of snake venom metalloproteinases.

Biomedica biochimica acta, 1992
The venoms of most Crotalidae snakes contain metalloproteinases which are the agents responsible for the production of venom-induced hemorrhage via proteolytic destruction of capillary basement membranes. Prevention of hemorrhage by administration of antiserum is generally not totally effective against damage at the site of envenomation.
A, Robeva   +4 more
openaire   +1 more source

Snake Venom Matrix Metalloproteinases (svMMPs)

2021
Inácio L. M. Junqueira-de-Azevedo   +1 more
openaire   +1 more source

BthMP: a new weakly hemorrhagic metalloproteinase from Bothrops moojeni snake venom

Toxicon, 2009
Mirian M Mendes   +2 more
exaly  

Pulmonary hemorrhage induced by jararhagin, a metalloproteinase from Bothrops jararaca snake venom

Toxicology and Applied Pharmacology, 2003
Teresa Escalante   +2 more
exaly  

Pathological alterations induced by neuwiedase, a metalloproteinase isolated from Bothrops neuwiedi snake venom

Biochimie, 2001
Veridiana M Rodrigues   +2 more
exaly  

Distribution of metalloproteinases and phospholipases A2 in snake venoms and relationship to venom toxicity

Toxicon, 2020
Noranathan da Costa Guimarães   +6 more
openaire   +1 more source

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