نتایج جستجو برای: toxin binding

تعداد نتایج: 463901  

Journal: :The Biochemical journal 1999
A Kuniyasu S Kawano Y Hirayama Y H Ji K Xu M Ohkura K Furukawa Y Ohizumi M Hiraoka H Nakayama

A peptide toxin isolated from the Chinese scorpion Buthus martensi Karsch (BmK-PL) stimulated Ca2+-release channel activity in both triad membranes and reconstituted ryanodine receptors partially purified from rabbit skeletal muscle. In [3H]ryanodine binding experiments, the toxin increased the affinity of ryanodine for the receptor, from a Kd of 24.3 nM to 2.9 nM, which is an enhancement simil...

Journal: :Microbiology 1997
Y Fujinaga K Inoue S Watanabe K Yokota Y Hirai E Nagamachi K Oguma

Binding of the purified type C 7S (neurotoxin), 12S and 16S botulinum toxins to epithelial cells of ligated small intestine or colon of the guinea pig (in vivo test) and to pre-fixed gastrointestinal tissue sections (in vitro test) was analysed. The 16S toxin bound intensely to the microvilli of epithelial cells of the small intestine in both in vivo and in vitro tests, but did not bind to cell...

Journal: :Journal of clinical microbiology 1987
B A McCardell J M Madden J T Stanfield B D Tall M J Stephens

Binding of cholera toxin to Giardia lamblia was demonstrated by two slightly different methods: an immunofluorescence technique using antibody to cholera toxin and anti-rabbit immunoglobulin G conjugated to fluorescein isothiocyanate, and a one-step fluorescence method in which G. lamblia was incubated with the B subunit of cholera toxin conjugated to fluorescein isothiocyanate.

2017
Sung-Min Kang Do-Hee Kim Ki-Young Lee Sung Jean Park Hye-Jin Yoon Sang Jae Lee Hookang Im Bong-Jin Lee

Toxin-antitoxin (TA) systems are essential for bacterial persistence under stressful conditions. In particular, Mycobacterium tuberculosis express VapBC TA genes that encode the stable VapC toxin and the labile VapB antitoxin. Under normal conditions, these proteins interact to form a non-toxic TA complex, but the toxin is activated by release from the antitoxin in response to unfavorable condi...

2013
Jeffrey M. Williams Takamasa Inoue Lindsey Banks Billy Tsai

Cholera toxin (CT) traffics from the host cell surface to the endoplasmic reticulum (ER), where the toxin's catalytic CTA1 subunit retrotranslocates to the cytosol to induce toxicity. In the ER, CT is captured by the E3 ubiquitin ligase Hrd1 via an undefined mechanism to prepare for retrotranslocation. Using loss-of-function and gain-of-function approaches, we demonstrate that the ER-resident f...

Journal: :The Journal of biological chemistry 1988
E Jover A Massacrier P Cau M F Martin F Couraud

Photoreactive derivatives of alpha- and beta-scorpion toxins have been used to analyze the subunit composition of Na+ channels in rat brain. In synaptosomes, both types of toxins preferentially labeled (greater than 85%) a component of 34,000 Da and, at a lower level, another component of 300,000 Da. Reduction of disulfide bridges shifted this latter band from 300,000 Da to 272,000 Da but did n...

Journal: :Journal of cell science 2001
O Kovbasnjuk M Edidin M Donowitz

Enterohemorrhagic Escherichia coli producing Shiga toxins 1 and/or 2 have become major foodborne pathogens. The specific binding of Shiga toxin 1 B-subunit to its receptor, a neutral glycolipid globotriaosylceramide Gb(3), on the apical surface of colonic epithelium followed by toxin entry into cells are the initial steps of the process, which can result in toxin transcytosis and systemic effec...

2018
Masato KoGuRE

As part of a study of the mechanism by which BaciUus thun'ngiensis nsecticidal crystal protein acts, a Bombyx mori receptor to the CryIA(a) toxin specific for lepidopterans was examined. Histolegical examination showed that the toxin acted on the brush-border membrane of the midgut columllar cells and broke its info}ding structure, causing cell lysis. The membrane vesicles were purified, and a ...

2018
Masato KoGuRE

As part of a study of the mechanism by which BaciUus thun'ngiensis nsecticidal crystal protein acts, a Bombyx mori receptor to the CryIA(a) toxin specific for lepidopterans was examined. Histolegical examination showed that the toxin acted on the brush-border membrane of the midgut columllar cells and broke its info}ding structure, causing cell lysis. The membrane vesicles were purified, and a ...

Journal: :Human vaccines & immunotherapeutics 2014
Mehdi Yousefi Roya Khosravi-Eghbal Ahmad Reza Mahmoudi Mahmood Jeddi-Tehrani Hodjatallah Rabbani Fazel Shokri

Tetanus is caused by the tetanus neurotoxin (TeNT), a 150 kDa single polypeptide molecule which is cleaved into an active two-chain molecule composed of a 50 kDa N-terminal light (L) and a 100 kDa C-terminal heavy (H) chains. Recently, extensive effort has focused on characterization of TeNT binding receptors and toxin neutralization by monoclonal antibodies (mAbs). Toxin binding inhibition and...

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