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pro vyhledávání: '"Stefaan De Boeck"'
Autor:
Daniël Broekaert, Tony Houthaeve, Kris Gevaert, Hans Demol, Joël Vandekerckhove, Magda Puype, Stefaan De Boeck
Publikováno v:
Electrophoresis. 18:2950-2960
We here describe a procedure for concentrating peptides from solutions by adsorbing them onto reverse-phase beads that were added to these solutions. The beads are then transferred to the target disc of the matrix assisted laser desorption ionization
Autor:
Stefaan De Boeck, Joël Vandekerckhove, Magda Puype, Kris Gevaert, Jean-Luc Verschelde, Jozef Van Damme, Marc Goethals
Publikováno v:
Electrophoresis. 17:918-924
A procedure is described for structural characterization and identification of proteins, purified by either one- or two-dimensional gel electrophoresis in the low picomole to femtomole range. The purified proteins are first detected in the primary ge
Autor:
Kris Gevaert, Marc Goethals, Bart Hoorelbeke, Hans Demol, Joël Vandekerckhove, Magda Puype, Lennart Martens, Jozef Van Damme, Stefaan De Boeck
Publikováno v:
Electrophoresis. 22(9)
Due to its very short analysis time, its high sensitivity and ease of automation, matrix-assisted laser desorption/ionization (MALDI)-peptide mass fingerprinting has become the preferred method for identifying proteins of which the sequences are avai
Autor:
Stefaan De Boeck, Kris Gevaert, Jozef Van Damme, Joël Vandekerckhove, Magda Puype, Marc Rider
Publikováno v:
Methods in Protein Structure Analysis ISBN: 9781489910332
One-dimensional (1-D) or two-dimensional (2-D) polyacrylamide gel electrophoresis is a convenient technique for purifying small amounts of proteins from very complex mixtures (O’Farrell, 1975; Celis & Bravo, 1984). For structural analysis, proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5b90ab6a10d4559f5a897679045e79e9
https://doi.org/10.1007/978-1-4899-1031-8_2
https://doi.org/10.1007/978-1-4899-1031-8_2
Publikováno v:
Biochimica et biophysica acta. 614(2)
The cholinesterase (acylcholine acylkhydrolase, EC 3.1.1.8) of chicken egg yolk was partly purified and characterized. It was compared to homologous enzymes of liver and blood plasma of laying hens. During gel filtration, yolk and liver cholinesteras
Autor:
Jan Stockx, Stefaan de Boeck
Publikováno v:
The International journal of biochemistry. 18(7)
Lysozyme accounts for 37% of the proteins of the hen's egg vitelline membrane. It can be extracted by salt solutions and purified by gel filtration on Sephadex G-50. There are no differences between the chemical and enzymic properties of egg white an
Publikováno v:
European journal of biochemistry. 52(1)
Chicken egg yolk contains an adenosine deaminase that was investigated after purifying about 500 times. It has a pH optimum at 6.5, aKm of 6.6 times 10(-5) mol/l and an approximate molecular weight of 14000; higher molecular forms could not be detect
Autor:
Jan Stockx, Stefaan de Boeck
Publikováno v:
The International journal of biochemistry. 18(7)
1. 1. Salt solutions and charged detergents are efficient solubilising agents for ovovitelline membrane lysozyme. 2. 2. Reassociation experiments with chemically modified lysozymes indicate that positively charged amino acid residues of lysozyme (the