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Selected new molecules were synthesized and purified in a parallel chemistry approach to determine structure activity relationships (SARs).
PAC was overexpressed in a genetically engineered Escherichia coli strain, secreted into the cultivation medium, harvested, and purified in a single step by anion-exchange chromatography.
Most of l-arabinose isomerases purified up to date employed the combination between DNA recombinant technology and affinity chromatography based on poly-histidine tail recognition, but few of the enzymes were obtained and purified in a non-recombinant way.
An abundantly secreted thermostable peptide (designed AcAFP) with a molecular mass of 5777 Da was isolated and purified in a previous work from a local strain of A. clavatus (VR1).
Crude culture filtrates were concentrated and purified in a rapid purification scheme described in the materials section.
This leads to the possibility that many different peptides or small molecules might be labeled and purified in a similar manner with subtle changes to achieve optimum yields.
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Recombinant AhpC was cloned, over-expressed and purified in an unmodified form and was also engineered to incorporate N and C-terminal mannose residues when expressed in the yeast Pichia pastoris.
Here we compared the antibody responses of rabbits to gp120 and gp140 that had been produced and purified in an identical manner.
Control plasmid of Myo117 with the similar size of S100A14 was a gift from Dr. Mariam Grigorian (Institute of Cancer Biology, Copenhagen, Denmark) to monitor for nonspecific effects which was expressed and purified in an identical manner [27].
All plasmid-encoded TorA/TorD His proteins were overproduced and purified in an identical manner.
Recombinant TTR was prepared and purified in an Escherichia coli expression system as described elsewhere [ 12].
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