Source:http://linkedlifedata.com/resource/pubmed/id/15581679
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-12-7
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pubmed:abstractText |
Two proteins G2a and G2b with molecular masses of approximately 24 kDa were isolated from Naja naja atra (Taiwan cobra) venom using sequential chromatography on gel filtration, ion-exchanger and reverse phase columns. The results of Edman degradation and mass analysis revealed that G2a is a cysteine-rich protein reported previously, and G2b is a novel polypeptide. CD spectra showed that the gross conformation of G2a and G2b notably differed. G2a exhibited an activity higher than that noted with G2b on inhibiting carbachol-induced muscle contraction. However, the two proteins weakly blocked muscle contraction evoked by K+. The observations that the two proteins exhibit the toxic activity in the concentration of micromolar range suggest that they are inherently weak toxins as other snake venom cysteine-rich proteins.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0041-0101
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15581679-Animals,
pubmed-meshheading:15581679-Bungarotoxins,
pubmed-meshheading:15581679-Chickens,
pubmed-meshheading:15581679-Circular Dichroism,
pubmed-meshheading:15581679-Cobra Venoms,
pubmed-meshheading:15581679-Muscle, Skeletal,
pubmed-meshheading:15581679-Muscle Contraction,
pubmed-meshheading:15581679-Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Purification and characterization of Taiwan cobra venom proteins with weak toxicity.
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pubmed:affiliation |
Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung 804, Taiwan, ROC. lschang@mail.nsysu.edu.tw
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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