Topic
Lysis
About: Lysis is a research topic. Over the lifetime, 6072 publications have been published within this topic receiving 216978 citations.
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TL;DR: It is demonstrated that, as the pH is lowered, two distinct changes in the physical properties of alpha-toxin occur, which are related to the acquisition of two new biological properties.
62 citations
TL;DR: This work has developed a two-step method to produce the grape dehydrin K(2) and YSK(2), which was shown to be more than 95% pure by reversed-phase high-performance liquid chromatography.
62 citations
61 citations
TL;DR: The treatment of Streptococcus sanguis with sodium lauroyl sarcosinate reduced cell hydrophobicity, and reduced the ability of the cells to coaggregate with Actinomyces spp.
Abstract: Summary: Incubating cells of Streptococcus sanguis with sodium lauroyl sarcosinate, under conditions that did not cause lysis, solubilized material comprising 5-8% of the cell dry weight. The treatment reduced cell hydrophobicity, and reduced the ability of the cells to coaggregate with Actinomyces spp. The extract contained about 20 polypeptides and these were identified as being cell-surface components on the basis of one or more of the following criteria: (a) being degraded when cells were incubated with protease; (b) being labelled when cells were iodinated using a lactoperoxidase-catalysed reaction; (c) reacting with antibodies raised to fixed whole cells. Eight of the polypeptides accounted for more than 70% of the total protein extracted, and one component (molecular mass 16 kDa) was hydrophobic. The cell-surface proteins described are implicated in cell hydrophobicity and coaggregation.
61 citations
TL;DR: A method was developed to measure the amounts of RNA polymerase subunits, α, β, β′ and σ in crude extracts of Escherichia coli, finding that all four subunits are fully conserved after bacteriophage T4 infection.
Abstract: A method was developed to measure the amounts of RNA polymerase subunits, α, β, β′ and σ in crude extracts of Escherichia coli. The proteins were labelled by growing the cells in 35S-sulphate containing media. For measuring β and β′, the cell lysate was electrophoresed on 6% polyacrylamide gels containing SDS and the β and β′ bands cut out and counted. For measuring α and σ, the cell lysate was co-electrophoresed with dansylated RNA polymerase on 8% polyacrylamide gels containing SDS. The fluorescent bands were cut out, the proteins eluted, and the α and σ subunits further purified on polyacrylamide gels containing 8 molar urea. The results are: (1) β′ is the subunit of the core RNA polymerase which is present in limiting amount. (2) The core enzyme, as measured by β′, constitutes a constant fraction of total cellular protein (0.9%), independent of the bacterial growth rate. (3) The α subunit is made in excess and is probably regulated independently. (4) The σ subunit is present in 0.3–0.4 times the amount of the core enzyme. (5) All four subunits are fully conserved after bacteriophage T4 infection.
61 citations