نتایج جستجو برای: toxin peptides

تعداد نتایج: 128988  

Journal: :The Biochemical journal 2004
Isabelle Huys Chen-Qi Xu Cheng-Zhong Wang Hélène Vacher Marie-France Martin-Eauclaire Cheng-Wu Chi Jan Tytgat

A novel HERG channel blocker was isolated from the venom of the scorpion Buthus martensi Karsch, sequenced and characterized at the pharmacological level after chemical synthesis. According to the determined amino acid sequence, the cDNA and genomic genes were then cloned. The genomic gene consists of two exons interrupted by an intron of 65 bp at position -6 upstream from the mature toxin. The...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1982
F Audibert M Jolivet L Chedid R Arnon M Sela

Three peptides corresponding to fragments of diphtheria toxin have been synthesized. They include the previously described tetradecapeptide and two structural analogs, the hexadecapeptide and the octadecapeptide. Conjugates of these peptides to proteins or a synthetic carrier have induced in guinea pig protection against the dermonecrotic activity of diphtheria toxin. All of the conjugates were...

2009
Linnaeus R Saravanan S Sambasivam Sathish Kumar

Cone snails are remarkable for the extent and diversity of gene-encoded peptide neurotoxins that are expressed in their venom apparatus. The protein content of the crude toxin extract of Conus figulinus Linneaus was found to be 1900 μg/mL. The crude extract (dilution up to 10) expressed hemolytic activity. The crude extract subjected to gel filtration chromatography yielded 60 fractions; the fr...

1997
James D. ASHCOM Bradley G. STILES

The venoms of predatory marine cone snails, Conus species, contain numerous peptides and proteins with remarkably diverse pharmacological properties. One group of peptides are the α­ conotoxins, which consist of 13–19 amino acids constrained by two disulphide bonds. A biologically active fluorescein derivative of Conus geographus α-conotoxin GI (FGI) was used in novel solution-phase-binding ass...

Journal: :Infection and immunity 1991
D X Sun J M Seyer I Kovari R A Sumrada R K Taylor

From a collection of monoclonal antibodies (MAbs) that recognize the native structure of the toxin-coregulated pilus of Vibrio cholerae, two protective MAbs (16.1 and 169.1) were used to localize the corresponding epitopes on the pilus. These MAbs were shown to specifically recognize the carboxyl half of the TcpA pilin subunit, as determined by their recognition of proteolytic fragments and hyb...

2014
Arvind Kannan G. Seshadri

Toxins from animal venoms are small peptides that recognize specific molecular targets in the brains of prey or predators. Next generation sequencing has uncovered thousands of diverse toxin sequences, but the functions of these peptides are poorly understood. Here we demonstrate that the use of machine learning techniques on sequence-derived features enables high accuracy in the task of predic...

Journal: :The Journal of clinical investigation 1996
C Pothoulakis R J Gilbert C Cladaras I Castagliuolo G Semenza Y Hitti J S Montcrief J Linevsky C P Kelly S Nikulasson H P Desai T D Wilkins J T LaMont

The intestinal effects of Clostridium difficile toxin A are inidated by toxin binding to luminal enterocyte receptors. We reported previously that the rabbit ileal brush border (BB) receptor is a glycoprotein with an alpha-d-galactose containing trisaccharide in the toxin-binding domain (1991. J. Clin. Invest. 88:119-125). In this study we characterized the rabbit ileal BB receptor for this tox...

Journal: :Bulletin of the Chemical Society of Japan 1986

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