Triton X-114 phase fractionation of an integral membrane surface protein mediating monoclonal antibody killing of Mycoplasma hyorhinis
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چکیده
منابع مشابه
Monoclonal antibody E8-18 identifies an integral membrane surface protein unique to Mycoplasma capricolum subsp. capripneumoniae.
Monoclonal antibody (MAb) E8-18 reacted with four isolates of Mycoplasma capricolum subsp. capripneumoniae in Western blots identifying an epitope on a 24 kDa antigen (p24). MAb E8-18 did not react with 11 isolates belonging to four other Mycoplasma species or subspecies closely related to M. capricolum subsp. capripneumoniae. A combination of trypsin treatment of intact organisms and detergent...
متن کاملPhase separation of integral membrane proteins in Triton X-114 solution.
A solution of the nonionic detergent Triton X-114 is homogeneous at 0 degrees C but separates in an aqueous phase and a detergent phase above 20 degrees C. The extent of this detergent phase separation increases with the temperature and is sensitive to the presence of other surfactants. The partition of proteins during phase separation in solutions of Triton X-114 is investigated. Hydrophilic p...
متن کاملThe characterization of plasma membrane-bound tubulin of cauliflower using Triton X-114 fractionation.
The cortical microtubules determine how cellulose microfibrils are deposited in the plant cell wall and are thus important for the control of cell expansion. To understand how microtubules can control microfibril deposition, the components that link the microtubules to the plasma membrane (PM) of plant cells must be isolated. To obtain information on the properties of the tubulin-membrane assoc...
متن کاملLipid-modified surface protein antigens expressing size variation within the species Mycoplasma hyorhinis.
Monoclonal antibodies (MAbs) previously shown to recognize distinct epitopes selectively expressed on the surface of some Mycoplasma hyorhinis strains were used to define two discrete sets of lipid-modified membrane surface proteins showing marked size variation within this species. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblot analysis of Triton X-114 phase-fractiona...
متن کاملFractionation of Tetrahymena ciliary membranes with triton X-114 and the identification of a ciliary membrane ATPase
Cilia were isolated from Tetrahymena thermophila, extracted with Triton X-114, and the detergent-soluble membrane + matrix proteins separated into Triton X-114 aqueous and detergent phases. The aqueous phase polypeptides include a high molecular mass polypeptide previously identified as a membrane dynein, detergent-soluble alpha and beta tubulins, and numerous polypeptides distinct from those f...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1987
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.55.5.1094-1100.1987