Phenyl Sepharose™ is used in protein chromatography, affinity chromatography, hydrophobic interaction media, resins and separation media. Phenyl Sepharose™ has been used in studies that contributed to improving industrial applications in additives in detergents and feed industries. Phenyl Sepharose™ has also been used to study microbial communities inhabiting hypersaline environments.
The Journal of biological chemistry, 270(1), 189-196 (1995-01-06)
The effect of cholesteryl ester transfer protein (CETP) on the size, composition, and structure of spherical, reconstituted HDL (rHDL) which contain apolipoprotein (apo) A-I as their sole apolipoprotein has been studied. Spherical rHDL were incubated with CETP and Intralipid for
The Journal of biological chemistry, 271(8), 4243-4250 (1996-02-23)
The effect of sphingomyelin (SPM) on the structure and function of discoidal and spherical reconstituted high density lipoproteins (rHDL) has been studied. Three preparations of discoidal rHDL with 1-palmitoyl-2-oleoyl phosphatidylcholine (POPC)/SPM/unesterified cholesterol (UC)/apolipoprotein (apo)A-I molar ratios of 99.6/0. 0/10.2/1.0, 86.0/13.6/10.8/1.0
Biochimica et biophysica acta, 1774(2), 286-296 (2007-01-16)
A gene eam in Clostridium difficile encodes a protein that is homologous to lysine 2,3-aminomutase (LAM) in many other species but does not have the lysyl-binding residues Asp293 and Asp330 in LAM from Clostridium subterminale SB4. The C. difficile protein
Lysine 2,3-aminomutase (LAM) from Clostridium subterminale SB4 catalyzes the interconversion of (S)-lysine and (S)-beta-lysine by a radical mechanism involving coenzymatic actions of S-adenosylmethionine (SAM), a [4Fe-4S] cluster, and pyridoxal 5'-phosphate (PLP). The enzyme contains a number of conserved acidic residues
Development of a downstream process for the isolation of <I>Staphylococcus aureus</I> arsenate reductase overproduced in <I>Escherichia coli</I>.
Messens, J., et al.
Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences, 737, 167-178 (2000)
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