Quantitation of the adsorption and penetration stages of bacteriophage φ6 infection
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2019, StructureCitation Excerpt :Absorbtion rate constants for other viruses presented in Table S1 were obtained from the following references: SMV1 (Uldahl et al., 2016), SSV9 (Bautista et al., 2015), and SIRV2 (Quemin et al., 2013). Bacteriophages: T1-T4 (Puck et al., 1951), ϕ6 (Olkkonen and Bamford, 1989), and PV22 (Zhilenkov et al., 2006). Halophilic archaeal viruses SH1, HHTV1 His1, and His2 (Svirskaite et al., 2016).
Asymmetrical flow field-flow fractionation in purification of an enveloped bacteriophage ϕ6
2018, Journal of Chromatography B: Analytical Technologies in the Biomedical and Life SciencesCitation Excerpt :Fractions (1 mL) were collected starting from the beginning of the elution gradient. Proteins were analysed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) using 15% (w/v) acrylamide in the separation gel [19] and Coomassie staining. Nucleic acids were visualized by ethidium bromide staining of the stacking gel.
Vesicle-like virion of Haloarcula hispanica pleomorphic virus 3 preserves high infectivity in saturated salt
2016, VirologyCitation Excerpt :In order to test HHPV3 sensitivity to these negative stains, 1× purified viruses were incubated in the undiluted stain solution (1:1) for the appropriate staining times (see above) at 22 °C, after which infectivity was determined by plaque assay. Virion components were analyzed using tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE; 16% acrylamide in the separation gel) (Olkkonen and Bamford, 1989). Gels were stained with Coomassie Brilliant Blue R 250 (Serva) for proteins and Sudan Black B (Sigma Aldrich) for lipids.
Asymmetric flow field flow fractionation methods for virus purification
2016, Journal of Chromatography ACitation Excerpt :The precipitated proteins were collected by centrifugation (Eppendorf centrifuge 5415D, 13,000 rpm, 30 min, 4 °C) and resuspended in 1.5 × SDS-PAGE sample buffer [42]. Boiled samples were analyzed in SDS polyacrylamide (SDS-PAGE) gels made in-house that used 16% acrylamide in the separation gels [42]. Proteins were visualized with Coomassie stain.