Results 211 to 220 of about 55,682 (249)
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Sequential polymerization of flagellin A and flagellin B into Caulobacter flagella
Journal of Molecular Biology, 1981The mode of polymerization of two species of flagellins, flagellin A and flagellin B, in polar flagella of Caulobacter crescentus was examined. By immunological staining we found that 1 to 1.2 μm of the portion of the flagellar filament proximal to the cell was composed of flagellin B, whereas about 5 μm of the distal portion was composed of flagellin ...
S, Koyasu, M, Asada, A, Fukuda, Y, Okada
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Purification and chemical properties of flagellin
Archives of Biochemistry and Biophysics, 1959Abstract A study of flagella and flagellin from six bacterial species led to the following generalizations: Flagella consist of proteins that, after removal from the cell bodies by shaking, can be isolated in highly purified condition by fractional centrifugation, or a combination of centrifugation and fractional precipitation with ammonium sulfate ...
T, KOBAYASHI, J N, RINKER, H, KOFFLER
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Purification of Native Flagellin
2019Flagella are effective organelles of locomotion and one of several virulence factors in Proteus mirabilis. To study their properties and role in virulence, we describe a protocol to extract and purify the native flagellin of P. mirabilis. Purified flagellin can be visualized by SDS-PAGE or immunoblot and is suitable for downstream applications such as ...
María José, González +3 more
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Relatedness of the flagellins from methanogens
Archives of Microbiology, 1992Purified flagellar filaments isolated from six methanogens were composed of multiple flagellins. Two flagellins were present in Methanococcus deltae (Mr = 34,000 and 32,000), Methanoculleus marisnigri (Mr = 31,000 and 25,500) and Methanococcus jannaschii (Mr = 31,000 and 27,500), three in Methanothermus fervidus (Mr = 34,000, 25,000 and 24,000) and ...
M L, Kalmokoff, S F, Koval, K F, Jarrell
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Flagellin Signalling in Plant Immunity
2007Like all higher living organisms, plants are constantly exposed to microbes that either grow epiphytically on the organ surface, establish beneficial interactions in specific tissues, or infect host tissues as pathogens and cause disease. In order to infect, pathogens must attach to the plant surface and break physical barriers to enter the tissue ...
Chinchilla, D., Boller, T., Robatzek, S.
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Flagellin as an object for supramolecular engineering
"Protein Engineering, Design and Selection", 1990A model of tertiary and quaternary structure of E. coli flagellin is suggested. According to this model, the molecule consists of two independent parts. One of them is formed by the N- and C-terminal regions of the polypeptide chain and is responsible for polymerization properties.
O V, Fedorov, A V, Efimov
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Medical Microbiology and Immunology, 1985
Ten antisera raised in rabbits, against polymeric flagellins from ten different Salmonella serotypes were used to determine the relative cross-activities between salmonella flagellins in monomeric form. The results showed a high degree of cross-reactivity between the antisera (IgG antibodies) and all monomeric flagellins investigated.
G F, Ibrahim +3 more
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Ten antisera raised in rabbits, against polymeric flagellins from ten different Salmonella serotypes were used to determine the relative cross-activities between salmonella flagellins in monomeric form. The results showed a high degree of cross-reactivity between the antisera (IgG antibodies) and all monomeric flagellins investigated.
G F, Ibrahim +3 more
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IMMUNE RESPONSE TO CHEMICALLY MODIFIED FLAGELLIN [PDF]
Flagellin (mol.wt. 40,000) from S. adelaide organisms and a series of acetoacetyl derivatives of flagellin were tested for their ability to induce humoral and cell-mediated immunity in adult rats. It was found that unmodified flagellin was an excellent inducer of antibody formation but a poor inducer of delayed-type hypersensitivity.
exaly +3 more sources
Molecular Microbiology, 2016
SummaryFliS chaperone binds to flagellin FliC in the cytoplasm and transfers FliC to a sorting platform of the flagellar type III export apparatus through the interaction between FliS and FlhA for rapid and efficient protein export during flagellar filament assembly. FliS also suppresses the secretion of an anti‐σ factor, FlgM.
Yukio, Furukawa +7 more
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SummaryFliS chaperone binds to flagellin FliC in the cytoplasm and transfers FliC to a sorting platform of the flagellar type III export apparatus through the interaction between FliS and FlhA for rapid and efficient protein export during flagellar filament assembly. FliS also suppresses the secretion of an anti‐σ factor, FlgM.
Yukio, Furukawa +7 more
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Science Signaling, 2001
Hayashi et al. characterized the transmembrane Toll-like receptor (TLR) 5 protein and identified a physiologically relevant ligand capable of activating TLR5 signaling. Overexpression of chimeric proteins consisting of the intracellular domain of TLR5 fused to the extracellular domain of CD4 (to promote dimerization)
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Hayashi et al. characterized the transmembrane Toll-like receptor (TLR) 5 protein and identified a physiologically relevant ligand capable of activating TLR5 signaling. Overexpression of chimeric proteins consisting of the intracellular domain of TLR5 fused to the extracellular domain of CD4 (to promote dimerization)
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