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: An exoenzyme which lyses intact cells, heat-killed cells, and cell walls of Arthrobacter crystallopoietes was purified 60-fold from the growth liquor obtained from a myxobacter (strain AL-1).
Abstract: Ensign, J. C. (University of Illinois, Urbana), and R. S. Wolfe. Lysis of bacterial cell walls by an enzyme isolated from a myxobacter. J. Bacteriol. 90:395–402. 1965.—An exoenzyme which lyses intact cells, heat-killed cells, and cell walls of Arthrobacter crystallopoietes was purified 60-fold from the growth liquor obtained from a myxobacter (strain AL-1). The lytic enzyme was produced during growth of the organism in a number of complex media, the maximal amount of enzyme being produced in yeast extract broth. The purified enzyme lysed at different rates a number of gram-positive bacteria. With the exception of Rhodospirillum rubrum, Spirillum itersonii, and S. serpens, the gram-negative bacteria tested were not attacked.
92 citations
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TL;DR: High yields of intracellular enzymes from yeast can be obtained by application of a series of electric field pulses with a flow process, which are higher than those obtained by mechanical disintegration or enzymatic lysis.
92 citations
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14 Jun 1995
TL;DR: A universal process for extracting and purifying nucleic acids from extremely small amounts of highly contaminated various biological and other starting materials is described in this article, which has applications in forensic medicine, medical diagnosis, molecular biology, biochemistry, genetic technology and all related fields.
Abstract: A universal process is disclosed for extracting and purifying nucleic acids from extremely small amounts of highly contaminated various biological and other starting materials. The invention has applications in forensic medicine, medical diagnosis, molecular biology, biochemistry, genetic technology and all related fields. The process is characterised in that nucleic acid-containing materials are lysed, the lysate is incubated with a non-porous, non-structured, highly disperse, homogeneous and chemically pure SiO2 substrate, the substrate is isolated with the bound nucleic acids and washed with a buffer solution, then the nucleic acids are dissolved from the substrate by a buffer with a lower salt concentration. Lysis of the material and nucleic acid immobilisation are preferably carried out in a reaction vessel. The substrate particles have a size of 7-40 nm, preferably 40 nm, and a specific surface from 50-300 g/m2, preferably 50 g/m2.
92 citations
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TL;DR: Evidence is provided that enzymes involved in the biosynthesis of two major lipid classes, the phosphatidylinositol mannosides (PIMs) and aminophospholipids, are compartmentalized within the plasma membrane, and that polar PIM biosynthesis occurs in the plasma membranes rather than the cell wall component of the PM-CW.
92 citations
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TL;DR: The microfluidic aqueous two-phase extraction forms the core component of an integrated lab-on-a-chip device comprising cell culture, lysis, purification and analysis on a single device, and does not require expensive affinity reagents or troublesome chromatographic steps.
Abstract: High-throughput screening assays of native and recombinant proteins are increasingly crucial in life science research, including fields such as drug screening and enzyme engineering. These assays are typically highly parallel, and require minute amounts of purified protein per assay. To address this need, we have developed a rapid, automated microscale process for isolating specific proteins from sub-microlitre volumes of E. Colicell lysate. Recombinant proteins are genetically tagged to drive partitioning into the PEG-rich phase of a flowing aqueous two-phase system, which removes ∼85% of contaminating proteins, as well as unwanted nucleic acids and cell debris, on a simple microfluidic device. Inclusion of the genetic tag roughly triples recovery of the autofluorescent protein AcGFP1, and also significantly improves recovery of the enzyme glutathione S-transferase (GST), from nearly zero recovery for the wild-type enzyme, up to 40% with genetic tagging. The extraction process operates continuously, with only a single step from cell lysate to purified protein, and does not require expensive affinity reagents or troublesome chromatographic steps. The two-phase system is mild and does not disrupt protein function, as evidenced by recovery of active enzymes and functional fluorescent protein from our microfluidic process. The microfluidic aqueous two-phase extraction forms the core component of an integrated lab-on-a-chip device comprising cell culture, lysis, purification and analysis on a single device.
91 citations