Crude culture filtrates were concentrated and purified in a rapid purification scheme described in the materials section.
Selected new molecules were synthesized and purified in a parallel chemistry approach to determine structure activity relationships (SARs).
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.
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).
Gas from pyrolyzer first was sent into the dust collector to remove the dust and then cooled and purified in a quench tower and electrical static oil collector, and tar was collected, simultaneously.
Briefly, 2 μg MBP, MBP-parkin or MBP-parkin mutants, expressed and purified in a E. coli expression system, was incubated with in vitro translated p62 (2 μg) in 50 μL ubiquitintion reaction buffer, containing 50 mmol/L Tris HCl [pH 7.5], 5 mmol/L MgCl2, 2 mmol/L DTT, 2 mmol/L ATP, 10 μg ubiquitin, 100 ng E1, and 200 ng E2 (UbcH7).
6X HIS tagged AtUBC8 was expressed and purified in a similar manner.
CifBp, CifPl and CifPa were all readily overexpressed and purified in a soluble form (see Materials and Methods).
