Characterization of the filamentous hemagglutin from Bordetella pertussis by gel electrophoresis

Lan, Birgit An der; Cowell, J L; Burstyn, Don G.; Manclark, C R; Chrambach, Andreas

doi:10.1007/bf00233802

Cited by 7 publications

(2 citation statements)

References 24 publications

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“…Other less dramatic arginine-rich sites in the FHA-deduced amino acid sequence may be secondary proteolytic cleavage sites, giving rise to the numerous lower molecular mass bands seen after storage of purified 220-kDa FHA polypeptide. This may explain previous reports that FHA is prone to proteolytic degradation (2,5).…”

Section: Methodssupporting

confidence: 71%

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Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence.

Relman

Domenighini

Tuomanen

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

312

214

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Section: Methodssupporting

confidence: 71%

“…Hemagglutinating activity for erythrocytes, including those of humans, is associated with the largest of these polypeptide species. FHA is a filamentous structure with dimensions of 2 nm x 40-100 nm (3,4), quite distinct from B. pertussis fimbriae (4,5).…”

mentioning

confidence: 99%

Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence.

Relman

Domenighini

Tuomanen

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

312

214

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Ferguson plots based on absolute mobilities in polyacrylamide gel electrophoresis: Dependence of linearity of polymerization conditions and application to the determination of free mobility

et al. 1988

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In contrast to Ferguson plots based on relative mobilities, Ferguson plots of proteins in polyacrylamide gel electrophoresis based on their absolute mobilities were found to be linear under unusual polymerization conditions which yield relatively wide gel fibers and a low total fiber length per unit weight, but not under previously and commonly used conditions. These linear Ferguson plots in gels of 1, 3 and 5% crosslinking intersect at a single gel concentration between 1 and 2% T (M-point). It is postulated that the measure of free mobility of the proteins is the M-point, and not the intercept of their Ferguson plots with the mobility axis as assumed previously. This postulate abolishes the well-known paradoxical interpretation of the increase with %C of the linearly extrapolated intercept of the Ferguson plot with the log(mobility) axis (designated Yo) in terms of free mobility. The postulate is also compatible with the interpretation of the points of intersection of the Ferguson plots of oligomeric series of proteins at finite gel concentrations (designated mu-points) as their common free mobilities.

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Information on DNA conformation derived from the Ferguson plot of DNA fragments of up to 9 kb in size, using polyacrylamide gel electrophoresis in a discontinuous buffer system

Orbán

Chrambach

1991

Electrophoresis

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The Ferguson plot in polyacrylamide gel electrophoresis (PAGE)(15%CDATD, moving boundary electrophoresis buffer system operative at pH 8.9, 4 degrees C, 8 mA/cm2 of gel) of DNA fragments up to 9.4 kb in size was found to exhibit a linear segment at polyacrylamide concentrations starting at 3% T and undergoing a gradual transition into a concave segment at higher gel concentrations, confirming previous findings by Stellwagen. The larger the DNA, and the higher the gel concentration, the less extended the linear and the more extended the concave segment of the plot. The lowest % T of the linear range for DNA in polyacrylamide remains unknown since mobilities at nongelling concentrations below 3% T have not as yet been measured. As previously suggested, the transition from the linear to the concave segment corresponds to that from the randomly oriented DNA to the anisotropically stretched, "reptating" DNA. For a DNA of 9.4 kb in size, the end of the linear range of the Ferguson plot can be extended from 3.5 to 5% T when 15% DATD rather than 2.5% Bis is used to crosslink the polyacrylamide. Increasing the temperature of PAGE from 4 degrees C to 25 and 50 degrees C widens the linear segment progressively, indicating an increasingly random orientation with rising temperature. When current density is increased from 8 to 40 mA/cm2, the concave curvature of the Ferguson plot of DNA 1 to 9.4 kb in size decreases, suggesting a transition from a "reptating" to a randomly distributed molecule, due to increased Joule heat.(ABSTRACT TRUNCATED AT 250 WORDS)

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Characterization of the filamentous hemagglutin from Bordetella pertussis by gel electrophoresis

Cited by 7 publications

References 24 publications

Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence.

Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence.

Ferguson plots based on absolute mobilities in polyacrylamide gel electrophoresis: Dependence of linearity of polymerization conditions and application to the determination of free mobility

Information on DNA conformation derived from the Ferguson plot of DNA fragments of up to 9 kb in size, using polyacrylamide gel electrophoresis in a discontinuous buffer system

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