نتایج جستجو برای: scorpion toxin

تعداد نتایج: 53607  

Journal: :Journal of biochemistry and molecular biology 2006
Maryam Nikkhah Hossein Naderi Manesh Majid Taghdir Mehdi Talebzadeh Majid Sadeghi Zadeh Janatan Schaller Mohamad N Sarbolouki

In this study, the cDNA of a new peptide from the venom of the scorpion, Buthotus saulcyi, was cloned and sequenced. It codes for a 64 residues peptide (Bsaul1) which shares high sequence similarity with depressant insect toxins of scorpions. The differences between them mainly appear in the loop1 which connects the beta-strand1 to the alpha-helix and seems to be functionally important in long ...

Journal: :European journal of biochemistry 2001
B Inceoglu J Lango J Wu P Hawkins J Southern B D Hammock

The venom of the South African scorpion Parabuthus transvaalicus was characterized using a combination of mass spectrometry and RP-HPLC separation and bioassays. The crude venom was initially separated into 10 fractions. A novel, moderately toxic but very high abundance peptide (birtoxin) of 58 amino-acid residues was isolated, identified and characterized. Each purification step was followed b...

2013
Zongyun Chen Bin Wang Jun Hu Weishan Yang Zhijian Cao Renxi Zhuo Wenxin Li Yingliang Wu

BACKGROUND Serine protease inhibitors act as modulators of serine proteases, playing important roles in protecting animal toxin peptides from degradation. However, all known serine protease inhibitors discovered thus far from animal venom belong to the Kunitz-type subfamily, and whether there are other novel types of protease inhibitors in animal venom remains unclear. PRINCIPAL FINDINGS Here...

2016
Michael Gurevitz Hagit Altman Gueta

Scorpion venom is rich in proteinaceous toxins that affect excitability by impeding ion channel gating. Channel blockers interact with the external region of the pore and obstruct ion conductance, whereas channel modifiers interact with the voltage sensor module hindering the activation or inactivation processes [1-3]. Scorpion toxin modifiers of voltage-gated sodium channels (Navs) are divided...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1975
W A Catterall

Four neurotoxins that activate the action potential Na+ ionophore of electrically excitable neuroblastoma cells interact with two distinct classes of sites, one specific for the alkaloids veratridine, batrachotoxin, and aconitine, and the second specific for scorpion toxin. Positive heterotropic cooperativity is observed between toxins bound at these two classes of sites. Tetrodotoxin is a nonc...

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