کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2499541 | 1116514 | 2006 | 7 صفحه PDF | دانلود رایگان |

As a first step to investigate the structure–function relationship of bothropstoxin-I (BthTX-I), a myotoxin from Bothrops jararacussu snake venom, our group previously cloned a recombinant toxin (rBthTX-I) in Escherichia coli. The aim of this work was to characterize the biological activities of this rBthTX-I (1.0 μM) in both phrenic-diaphragm and extensor digitorum longus preparations in vitro, by means of myographic and morphologic techniques. Native BthTX-I (1.0 μM) was used as a standard. The influence of heparin (27.5 μg/ml) upon the biological activities of both toxins was also investigated. rBthTX-I had similar effects to the native toxin inducing blockage of both directly and indirectly evoked contractions in phrenic-diaphragm preparations, and muscle damage characterized by edema, round fibers, and cell areas devoid of myofibrils. Interestingly the paralyzing activity of rBthTX-I was slightly more potent than the native toxin. Heparin prevented paralyzing and myotoxic effects of both the native and recombinant toxins. This work shows that rBthTX-I was expressed in a fully active form, and presents a biological profile similar to the native toxin.
Journal: Experimental and Toxicologic Pathology - Volume 57, Issue 3, 20 January 2006, Pages 239–245