Article
Purification and characterization of a phospholipase A2 isoenzyme isolated from Lachesis muta snake venom.
Departamento de Bioquímica Médica, Instituto de Ciências Biomédicas, Universidade Federal do Rio de Janeiro, RJ, Rio de Janeiro, Brazil.
Biochemical Pharmacology (impact factor:
4.7).
06/2002;
63(9):1589-97.
DOI:10.1016/S0006-2952(02)00873-0
pp.1589-97
Source: PubMed
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Citations (0)
- Cited In (5)
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Article: Comparative analysis of viperidae venoms antibacterial profile: a short communication for proteomics.
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ABSTRACT: Bacterial infections involving multidrug-resistant strains are one of the ten leading causes of death and an important health problem in need for new antibacterial sources and agents. Herein, we tested and compared four snake venoms (Agkistrodon rhodostoma, Bothrops jararaca, B. atrox and Lachesis muta) against 10 Gram-positive and Gram-negative drug-resistant clinical bacteria strains to identify them as new sources of potential antibacterial molecules. Our data revealed that, as efficient as some antibiotics currently on the market (minimal inhibitory concentration (MIC) = 1-32 μg mL(-1)), A. rhodostoma and B. atrox venoms were active against Staphylococcus epidermidis and Enterococcus faecalis (MIC = 4.5 μg mL(-1)), while B. jararaca inhibited S. aureus growth (MIC = 13 μg ml(-1)). As genomic and proteomic technologies are improving and developing rapidly, our results suggested that A. rhodostoma, B. atrox and B. jararaca venoms and glands are feasible sources for searching antimicrobial prototypes for future design new antibiotics against drug-resistant clinical bacteria. They also point to an additional perspective to fully identify the pharmacological potential of these venoms by using different techniques.Evidence-based Complementary and Alternative Medicine 10/2008; 2011:960267. · 4.77 Impact Factor -
Article: Interactions of PLA2-s from Vipera lebetina, Vipera berus berus and Naja naja oxiana Venom with Platelets, Bacterial and Cancer Cells.
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ABSTRACT: Secretory phospholipasesA(2) (sPLA(2)s) form a large family of structurally related enzymes widespread in nature. Herein, we studied the inhibitory effects of sPLA(2)s from Vipera lebetina (VLPLA(2)), Vipera berus berus (VBBPLA(2)), and Naja naja oxiana (NNOPLA(2)) venoms on (i) human platelets, (ii) four different bacterial strains (gram-negative Escherichia coli and Vibrio fischeri; gram-positive Staphylococcus aureus and Bacillus subtilis) and (iii) five types of cancer cells (PC-3, LNCaP, MCF-7, K-562 and B16-F10) in vitro. sPLA(2)s inhibited collagen-induced platelet aggregation: VBBPLA(2) IC(50) = 0.054, VLPLA(2) IC(50) = 0.072, NNOPLA(2) IC(50) = 0.814 μM. p-Bromophenacylbromide-inhibited sPLA(2) had no inhibitory action on platelets. 36.17 μM VBBPLA(2 )completely inhibited the growth of gram-positive Bacillus subtilis whereas no growth inhibition was observed towards gram-negative Escherichia coli. The inhibitory action of sPLA(2)s (~0.7 μM and ~7 μM) towards cancer cells depended on both venom and cell type. VBBPLA(2 )(7.2 μM) inhibited significantly the viability of K-562 cells and the cell death appeared apoptotic. The sPLA(2)s exhibited no inhibitory effect towards LNCaP cells and some effect (8%-20%) towards other cells. Thus, already sub-μM concentrations of sPLA(2)s inhibited collagen-induced platelet aggregation and from the current suite of studied svPLA(2)s and test cells, VBBPLA(2) was the most growth inhibitory towards Bacillus subtilis and K-562 cells.Toxins. 01/2013; 5(2):203-23. -
Article: WITHDRAWN: Antiophidian properties of a dolastane diterpene isolated from the marine brown alga Canistrocarpus cervicornis.
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ABSTRACT: The Publisher regrets that this article is an accidental duplication of an article that has already been published, http://dx.doi.org/10.1016/j.bionut.2011.06.021. The duplicate article has therefore been withdrawn.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 10/2010; · 2.24 Impact Factor
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Keywords
amino terminal sequence
apparent molecular mass
biological activities
dependent
gel filtration
homology
indirect hemolytic activity
LM-PLA2-II
new phospholipase A2
p-bromophenacyl bromide
PLA2
PLA2s
platelet aggregation induced
potent inhibitory effect
Pretreatment
reverse-phase chromatography
Sephacryl S-200 HR column
significant paw edema reaction
single polypeptide chain
