pubmed-article:21544178 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21544178 | lifeskim:mentions | umls-concept:C0037380 | lld:lifeskim |
pubmed-article:21544178 | lifeskim:mentions | umls-concept:C0206301 | lld:lifeskim |
pubmed-article:21544178 | lifeskim:mentions | umls-concept:C0012238 | lld:lifeskim |
pubmed-article:21544178 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:21544178 | lifeskim:mentions | umls-concept:C0597304 | lld:lifeskim |
pubmed-article:21544178 | pubmed:dateCreated | 2011-5-5 | lld:pubmed |
pubmed-article:21544178 | pubmed:abstractText | Testing whether venoms may aid in digestion of the prey, eleven snake venoms were compared for the presence of proteases and endopeptidases that function in alkaline pH conditions. In vitro experiments examined the relative protease and endopeptidase activity of the venoms, which involved combining bovine muscle and snake venom in a buffered solution, encased within dialysis tubing. This mixture was then incubated at room temperature (?20°C) for 24hr, with constant shaking. Bicinchoninic acid (BCA) assay and ninhydrin assay were used to determine peptide and amino acid concentrations. Histological and immunohistochemical investigations using N. kaouthia venom confirmed in vitro findings. Results show that B. arietans venom generated the highest amount of protein/peptides and amino acids in the dialysates, while O. scutellatus, N. ater niger and P. textilis venom did not show any significant protein degradation under alkaline conditions. Histological examination revealed varying degrees of muscle cell damage for each of the venom investigated, and the immunohistochemical study on N. kaouthia venom showed that the venom penetrated the muscle tissue to a significant degree. In vitro assays and histological results indicate that particular venoms may possess the ability to enhance digestion of bovine muscle tissue. | lld:pubmed |
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pubmed-article:21544178 | pubmed:language | eng | lld:pubmed |
pubmed-article:21544178 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21544178 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
pubmed-article:21544178 | pubmed:issn | 2044-0324 | lld:pubmed |
pubmed-article:21544178 | pubmed:author | pubmed-author:MirtschinPete... | lld:pubmed |
pubmed-article:21544178 | pubmed:author | pubmed-author:MadarasFrankF | lld:pubmed |
pubmed-article:21544178 | pubmed:author | pubmed-author:BottrallJoshu... | lld:pubmed |
pubmed-article:21544178 | pubmed:author | pubmed-author:BivenChristop... | lld:pubmed |
pubmed-article:21544178 | pubmed:author | pubmed-author:VenningMichae... | lld:pubmed |
pubmed-article:21544178 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21544178 | pubmed:volume | 1 | lld:pubmed |
pubmed-article:21544178 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21544178 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21544178 | pubmed:pagination | 18-28 | lld:pubmed |
pubmed-article:21544178 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
pubmed-article:21544178 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:21544178 | pubmed:articleTitle | Proteolytic activity of Elapid and Viperid Snake venoms and its implication to digestion. | lld:pubmed |
pubmed-article:21544178 | pubmed:publicationType | Journal Article | lld:pubmed |