نتایج جستجو برای: toxin binding

تعداد نتایج: 463901  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1983
R I Norman A Schmid A Lombet J Barhanin M Lazdunski

The gating component associated with the voltage-sensitive Na+ channel from electroplax membranes of Electrophorus electricus has been purified by using toxin gamma from the venom of the scorpion Tityus serrulatus serrulatus. The toxin-binding site was efficiently solubilized with Lubrol PX, resulting in an extract of high initial specific activity. Purification was achieved by adsorption of th...

2016
Zishan Zhou Zeyu Wang Yuxiao Liu Gemei Liang Changlong Shu Fuping Song Xueping Zhou Alejandra Bravo Mario Soberón Jie Zhang

Cry1Ac toxin-binding proteins from Helicoverpa armigera brush border membrane vesicles were identified by an improved pull-down method that involves coupling Cry1Ac to CNBr agarose combined with liquid chromatography-tandem mass spectrometry (LC-MS/MS). According to the LC-MS/MS results, Cry1Ac toxin could bind to six classes of aminopeptidase-N, alkaline phosphatase, cadherin-like protein, ATP...

Journal: :Molecular pharmacology 1988
Y Yajima Y Akita T Saito

The effects of cholera toxin on the coupling of the thyrotropin-releasing hormone (TRH) receptor to a guanine nucleotide-binding (G) protein were examined in a GH3 clonal strain of rat pituitary tumor cells. Incubation of the cells with cholera toxin (50 ng/ml) for 16 hr caused a decrease in [3H]methyl-TRH binding to 59% of the control level and in TRH-stimulated low Km GTPase activity from 143...

2001
John Collier

Prior studies have described two functionally distinct ligand-binding sites on whole diphtheria toxin, the NAD site, which catalyzes the intracellular ADP-ribosylation reaction, and the P site, which affects toxin binding to sensitive cells. Occupancy of the P site by ATP or other phosphorylated compounds inhibits toxin attachment to cells. Here we show that binding of NAD site and P site ligan...

Journal: :vaccine research 0
f sadeghpour heravi pertussis reference laboratory‚ department of bactriology, pasteur institute of iran, tehran, iran vs nikbin pertussis reference laboratory‚ department of bactriology, pasteur institute of iran, tehran, iran f shahcheraghi pertussis reference laboratory‚ department of bactriology, pasteur institute of iran, tehran, iran

introduction: despite high level of vaccination against pertussis‚ whooping cough has re-emerged as a health threat, especially in infants. this could be related to expansion of bordetella pertussis with novel alleles for virulence factors including the pertussis toxin promoter, ptxp3. compared to ptxp1 strains‚ ptxp3 strains produce more pertussis toxin which results in immune suppression and ...

Journal: :Cell 2002
Frank Breinig Donald J. Tipper Manfred J. Schmitt

Saccharomyces cerevisiae K1 killer strains are infected by the M1 double-stranded RNA virus encoding a secreted protein toxin that kills sensitive cells by disrupting cytoplasmic membrane function. Toxin binding to spheroplasts is mediated by Kre1p, a cell wall protein initially attached to the plasma membrane by its C-terminal GPI anchor. Kre1p binds toxin directly. Both cells and spheroplasts...

Journal: :The Journal of biological chemistry 1980
N P Morris E Consiglio L D Kohn W H Habig M C Hardegree T B Helting

Fragment C of tetanus toxin appears to retain most of the determinants of the tetanus toxin molecule insofar as interactions with neural or thyroid membranes and with gangliosides are concerned. Thus, unlabeled fragment C is nearly as effective as unlabeled tetanus toxin in inhibiting the binding of either ‘251-labeled toxin or ‘251-labeled thyrotropin to neural or thyroid membranes. ‘251-label...

Journal: :Infection and immunity 1986
G Fuchs M Mobassaleh A Donohue-Rolfe R K Montgomery R J Grand G T Keusch

This study examined the binding of purified 125I-labeled shigella toxin to rabbit jejunal microvillus membranes (MVMs). Toxin binding was concentration dependent, saturable, reversible, and specifically inhibited by unlabeled toxin. The calculated number of toxin molecules bound at 4 degrees C was 7.9 X 10(10) (3 X 10(10) to 2 X 10(11))/micrograms of MVM protein or 1.2 X 10(6) per enterocyte. S...

Journal: :Infection and immunity 1982
H Tolleshaug R Skjelkvåle T Berg

Binding of enterotoxin from Clostridium perfringens type A was studied in suspensions of parenchymal and nonparenchymal cells from rat liver. In hepatocytes, 1.5 X 10(6) specific binding sites per cell with an association constant of 3.2 X 10(6) M-1 were found. About 1% of the added toxin was nonspecifically bound to the hepatocytes. At concentrations of toxin below 0.1 micrograms/ml, 80% of th...

2014
Yo Sugawara Masahiro Yutani Sho Amatsu Takuhiro Matsumura Yukako Fujinaga Eric A. Johnson

Botulinum neurotoxin (BoNT) inhibits neurotransmitter release in motor nerve endings, causing botulism, a condition often resulting from ingestion of the toxin or toxin-producing bacteria. BoNTs are always produced as large protein complexes by associating with a non-toxic protein, non-toxic non-hemagglutinin (NTNH), and some toxin complexes contain another non-toxic protein, hemagglutinin (HA)...

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