Source:http://linkedlifedata.com/resource/pubmed/id/18501940
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
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| pubmed:dateCreated |
2008-6-9
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| pubmed:abstractText |
BmTX-I, an Asp49 phospholipase A(2), was purified from Bothrops moojeni venom after only one chromatographic step using reverse-phase HPLC on mu-Bondapak C-18 column. A molecular mass of 14238.71Da was determined by MALDI-TOF mass spectrometry. Amino acid analysis showed a high content of hydrophobic and basic amino acids as well as 14 half-cysteine residues. The BmTX-I PLA(2) had a sequence of 121 residues of amino acids: DLWQFNKMIK KEVGKLPFPF YGAYGCYCGW GGRGEKPKDG TDRCCFVHDC CYKKLTGCPK WDDRYSYSWK DITIVCGEDL PCEEICECDR AAAVCFYENL GTYNKKYMKH LKPCKKADYP C and pI value 7.84, and showed a high degree of homology with basic Asp49 PLA(2) myotoxins from other Bothrops venoms. BmTX-I presented PLA(2) activity in the presence of a synthetic substrate and showed a minimum sigmoidal behavior, reaching its maximal activity at pH 8.0 and 35-45 degrees C. Maximum PLA(2) activity required Ca(2+) and in the presence of Mg(2+), Cd(2+) and Mn(2+) it was reduced in presence or absence of Ca(2+). Crotapotin from Crotalus durissus colillineatus rattlesnake venom has significantly inhibited (P<0.05) the enzymatic activity of BmTX-I. In vitro, the whole venom and BmTX-I caused a blockade of the neuromuscular transmission in young chick biventer cervicis preparations in a similar way to other bothrops species. In mice, BmTX-I and the whole venom-induced myonecrosis and a systemic interleukin-6 response upon intramuscular injection. Edema-forming activity was also analyzed through injection of the venom and the purified BmTX-I into the subplantar region of the right footpad. Since BmTX-I exert a strong proinflammatory effect; the enzymatic phospholipids hydrolysis might be relevant for these phenomena.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Crotalid Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Crotoxin,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/myotoxin II, Bothrops moojeni
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0041-0101
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
51
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1509-19
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| pubmed:meshHeading |
pubmed-meshheading:18501940-Amino Acid Sequence,
pubmed-meshheading:18501940-Animals,
pubmed-meshheading:18501940-Bothrops,
pubmed-meshheading:18501940-Chemical Fractionation,
pubmed-meshheading:18501940-Chickens,
pubmed-meshheading:18501940-Chromatography, High Pressure Liquid,
pubmed-meshheading:18501940-Crotalid Venoms,
pubmed-meshheading:18501940-Crotalus,
pubmed-meshheading:18501940-Crotoxin,
pubmed-meshheading:18501940-Kinetics,
pubmed-meshheading:18501940-Male,
pubmed-meshheading:18501940-Mice,
pubmed-meshheading:18501940-Molecular Sequence Data,
pubmed-meshheading:18501940-Neuromuscular Blockade,
pubmed-meshheading:18501940-Neurotoxins,
pubmed-meshheading:18501940-Phospholipases A,
pubmed-meshheading:18501940-Sequence Alignment,
pubmed-meshheading:18501940-Sequence Analysis, Protein,
pubmed-meshheading:18501940-Spectrometry, Mass, Matrix-Assisted Laser...
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| pubmed:year |
2008
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| pubmed:articleTitle |
Biological and biochemical characterization of new basic phospholipase A(2) BmTX-I isolated from Bothrops moojeni snake venom.
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| pubmed:affiliation |
Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas, Campinas, SP, Brazil.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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