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Gel electrophoresis

About: Gel electrophoresis is a research topic. Over the lifetime, 26026 publications have been published within this topic receiving 1113565 citations.


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Journal ArticleDOI
01 Jan 1996-Planta
TL;DR: Purified recombinant Bet v 1 was shown to degrade plant RNA and the monomer and the dimer of Bet v1 showed RNase activity.
Abstract: The major birch (Betula alba L.) pollen allergen, Bet v 1, has been shown to be homologous to pathogenesis-related proteins in a number of plants. Recently, it was demonstrated that a ginseng protein with high homology to an intracellular pathogenesis-related protein of parsley and to Bet v 1 is a ribonuclease (RNase). Birch pollen extract was separated in an RNase activity gel. Four major RNase bands were excised from the gel, reseparated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and identified by Western blotting with a specific Bet v 1 monoclonal antibody and patient's serum. Thus the monomer and the dimer of Bet v 1 showed RNase activity. Purified recombinant Bet v 1 was shown to degrade plant RNA. The RNase activity of recombinant Bet v 1 was 180 units · mg−1.

182 citations

Journal ArticleDOI
A.R.J. Bakkenist1, Ron Wever1, T. Vulsma1, H. Plat1, B.F. Van Gelder1 
TL;DR: The circular dichroism spectra of ferric and ferrous myeloperoxidase in the visible and ultraviolet region show maxima and minima in ellipticity.

182 citations

Journal ArticleDOI
TL;DR: The motility stimulation of the fibrosarcoma cells with AMF is associated with the phosphorylation of the AMF receptor, a 78-kDa cell surface glycoprotein (gp78), suggesting protein kinase participation in migratory signal transduction.

182 citations

Journal ArticleDOI
TL;DR: It is demonstrated that apo-E is synthesized as preprotein and undergoes intracellular proteolysis and glycosylation and extracellular desialation to attain the major asialoapo- E isoprotein form observed in plasma.

182 citations

Journal ArticleDOI
TL;DR: The results demonstrated that heat-labile antigenic specificity was conferred on C. jejuni VC74 by an outer membrane protein with an approximate molecular weight of 92,500 and both the major outer membraneprotein and the flagella were immunogenic but did not confer either strain or species serospecificity on the strains tested.
Abstract: The technique of immunoblotting was used to identify the surface protein antigens of Campylobacter jejuni. Polyclonal antisera were raised in rabbits to formalinized cells of a typical human fecal isolate, C. jejuni VC74. Surface components were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Fractions analyzed included whole cell lysates, sarcosinate-extracted outer membranes, released outer membrane blebs (fragments), isolated flagella, 0.2 M glycine-hydrochloride (pH 2.2) extract, saline extract, and material released by osmotic shocking. The ability of the antisera to recognize corresponding antigens on other strains of thermophilic campylobacters and Campylobacter fetus was also determined. The results demonstrated that heat-labile antigenic specificity was conferred on C. jejuni VC74 by an outer membrane protein with an approximate molecular weight of 92,500. Both the major outer membrane protein and the flagella were immunogenic but did not confer either strain or species serospecificity on the strains tested. Another major antigen on thermophilic campylobacter cells was a surface protein with an approximate molecular weight of 31,000. This common antigen was preferentially removed by glycine extraction but was not detectable in outer membrane prepared by sarcosinate extraction.

182 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202364
2022116
2021108
2020104
2019120
2018147