Results 201 to 210 of about 51,201 (249)

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, B, Dragulev, J, Perales, J W, Fox, G B, Domont   +4 more
openaire   +2 more sources

Bacterial Expression of a Snake Venom Metalloproteinase Inhibitory Protein from the North American Opossum (D. Virginiana).

Toxicon, 2021
R. M. Werner, Lauren M Miling, Brianna M Elliot, Mitchell R Hawes, Jennifer M. Wickens, D. E. Weber   +5 more
semanticscholar   +1 more source

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

Toxicon, 2009
In this work, a new weakly hemorrhagic metalloproteinase (BthMP) was purified from Bothrops moojeni snake venom. This enzyme was homogeneous by native and SDS-PAGE. It showed a polypeptide chain of 23.5kDa, pI=7.1, and N-terminal blocked. BthMP is comprised of high proteolytic activity on casein, fibrin and bovine fibrinogen, with no coagulating ...
Mário Sérgio R, Gomes, Mirian M, Mendes, Fábio, de Oliveira, Rodrigo M, de Andrade, Carolina P, Bernardes, Amélia, Hamaguchi, Tânia M, de Alcântara, Andreimar M, Soares, Veridiana M, Rodrigues, Maria I, Homsi-Brandeburgo   +9 more
openaire   +2 more sources

Potent histamine-releasing activity of atrahagin, a novel snake venom metalloproteinase

The International Journal of Biochemistry & Cell Biology, 2006
Poisonous snakebite wound is a popular disease worldwide. However, the pathogenesis remains unclear. In the present study, a novel metalloproteinase atrahagin in Chinese cobra (Naja atra) snake venom was purified, using heparin-sepharose followed by Superdex 75 gel filtration chromatography.
Ji-Fu, Wei, Ya-Zhen, Mo, Li-Ya, Qiao, Xiao-Long, Wei, Han-Qiu, Chen, Hua, Xie, Yi-Ling, Fu, Wan-Yu, Wang, Yu-Liang, Xiong, Shao-Heng, He   +9 more
openaire   +2 more sources

PO41, a snake venom metalloproteinase inhibitor isolated from Philander opossum serum

Toxicon, 2003
PO41 was isolated from Philander opossum serum by DEAE-Sephacel, Phenyl Superose and Superdex 200 chromatographies and showed a molecular mass of 41,330 Da by MALDI-TOF MS. Molecular masses of 81.5 and 84.5 kDa were obtained by size exclusion chromatography and dynamic laser light scattering, respectively, suggesting that PO41 is dimeric.
Patrícia B, Jurgilas, Ana G C, Neves-Ferreira, Gilberto B, Domont, Jonas, Perales   +3 more
openaire   +2 more sources

Snake Venom Metalloproteinases

2021
Charlotte A. Dawson, Stuart Ainsworth, Laura-Oana Albulescu, Nicholas R. Casewell   +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, V, Politi, J D, Shannon, J B, Bjarnason, J W, Fox   +4 more
openaire   +1 more source

[Snake venom metalloproteinases: structure, biosynthesis and function(s)].

Archives de l'Institut Pasteur de Tunis, 2011
The biochemical and the pharmacological characterization of snake venoms revealed an important structural and functional polymorphism of proteins which they contain. Among them, snake venom metalloproteases (SVMPs) constitute approximatively 20 to 60% of the whole venom proteins.
I, Limam, M, El Ayeb, N, Marrakchi
openaire   +1 more source

The chemistry of snake venom and its medicinal potential

Nature Reviews Chemistry, 2022
Ana Oliveira, Matilde F Viegas, Saulo Luís Da Silva   +2 more
exaly  

Eepression and characterization of a recombinant novel snake venom metalloproteinase from green pit viper (Cryptelytrop albolabris)

Snake venom metaloproteases (SVMPs) may degrade extracellular matrix and/or clotting factors, as well as inhibit integrin and platelet functions, studying them not only gives US deeper insights in pathogenesis of snakebites, but also potentially yields ...
Panchalee Jangprasert
semanticscholar   +1 more source