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Sentences for "chromatography "
mori BBMV proteins were separated by Q Sepharose anion-exchange chromatography and all eluted fractions were tested for APN enzymatic activity.
All column chromatography was carried out on an ÄKTA Explorer (Amersham Pharmacia Biotech).
Following ether extraction, samples were dissolved in ethyl acetate and spotted onto thin layer chromatography plates.
Size exclusion chromatography of lysates prepared from cells harboring epitope-tagged Pcu3p or CSN subunits at the endogenous genomic loci, revealed precise co-elution of Pcu3p with CSN subunits 1, 3, 4, and 5 in high molecular weight fractions corresponding to approximately 550 kDa (Fig.
The presence of p35 in high molecular weight fraction (~670 kDa) following superose 12 gel filtration chromatography strengthen this hypothesis and clearly suggests that p35 forms an oligomeric structure.
(2) The total amounts of the mutants isolatable after chromatography were compared with wild-type L1 levels.
Heparin and HS in the conditioned media with affinity for PEDF GAGs and polyanions in the CM were fractionated by anion-exchange column chromatography followed by PEDF-affinity column chromatography (Fig.
4 micron membrane and its soluble components subjected to anion-exchange column chromatography using Q-Sepharose Fast Flow (1 ml bed volume).
PEDF-affinity column chromatography To identify components with PEDF-binding affinity, purified recombinant protein was used to prepare PEDF-affinity resin with 3 M Emphaze™ Biosupport Medium (Pierce Chemical) [ 18 ] .
The mixture was packed into a 10 ml Polyprep chromatography column (Bio-Rad) and washed with 10-column volumes of buffer P.
Phospholipids were separated by chromatography in 100:75:7:4 of chloroform:methanol:acetic acid:water.
One way in which integrins were originally shown to be fibronectin receptors was by affinity chromatography of radioiodinated cell surface proteins on a fibronectin column [ 27 28 ] .
Consistent with these earlier studies, cell surface radioiodination of RASMCs followed by affinity chromatography on fibronectin Sepharose and elution with EDTA revealed the binding of two major bands at 120 kDa and 140 kDa (Fig.
These sizes match those of the ß1 and ?
5 integrin submits, respectively, that have been shown by affinity chromatography to bind to the cell binding domain (i.
Affinity chromatography on a III1-C Sepharose column revealed the binding of three major bands of sizes 120 kDa, 140 kDa and 150 kDa (Fig.
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