Examples of 'proteins were purified' in a sentence

Meaning of "proteins were purified"

proteins were purified: Refers to the process of removing impurities or unwanted substances from proteins, typically done in laboratory settings for research or experimentation purposes

How to use "proteins were purified" in a sentence

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proteins were purified
Both proteins were purified to homogeneity by conventional chromatography.
Only highly glycosylated proteins were purified for use.
The proteins were purified by glutathione affinity chromatography.
All the recombinant polyepitope carrier proteins were purified using a similar strategy.
Proteins were purified using affinity chromatography.
The bacterially expressed proteins were purified over an amylose affinity column.
Proteins were purified from filtered cell culture supernatants.
This comparison demonstrated that similar proteins were purified by the two methods.
The proteins were purified as above.
After enrichment over the Ni-NTA column, the proteins were purified by gel filtration.
The encoded proteins were purified using column chromatography.
Then, antibody columns were produced using the selected será and the antigen proteins were purified.
The fusión proteins were purified as described below.
These constructs were expressed in E. coli and the proteins were purified for binding assays.
The recombinant proteins were purified and used to vaccinate mice.

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The induced cells were collected 3 hours later and the proteins were purified on a Nickel column.
These recombinant proteins were purified and used for immunization.
Proteins were purified as described above.
The soluble receptor proteins were purified over a protein A column.
Proteins were purified as follows.
In one study, fusión proteins were purified as follows.
The proteins were purified by affinity chromatography using glutathione sepharose beads.
Lysogens were prepared and the induced proteins were purified by anti-IFN-gamma receptor immunoadsorbent.
Proteins were purified from filtered cell culture supernatants referring to standard protocols.
After a large-scale fermentation, proteins were purified and used for monoclonal antibody production.
Proteins were purified from the cell culture supernatant vía Protein-A and size exclusion chromatography.
Expression was in E. coli and the proteins were purified by gel chromatography, as before.
The proteins were purified as described in the Methods section.
Figure 1A illustrates how the antimicrobial proteins were purified by gel filtration chromatography.
Expressed proteins were purified by conventional chromatography using standard buffers.
After 3.5 h, transformants were sonicated and the overexpressed proteins were purified according to the manufacturers instructions.
The resulting proteins were purified using immobilized metal affinity chromatography.
After periplasmic extraction, dAb fusión proteins were purified vía the C-terminal His6 tag.
Fusion proteins were purified by the use of Glutathion sepharose and subsequently cleaved with thrombin.
The control Ra12 and TRX proteins were purified in a similar manner.
The proteins were purified in a single step by protein A affinity chromatography.
Recombinant human ERa and ERB proteins were purified from transfected Sf9-cells.
Fusion proteins were purified from the culture medium using protein G affinity chromatography.
The latter two proteins were purified to a high degree.
The proteins were purified by one-step affinity chromatography using glutathione-agarose.
Once identified the proteins were purified by ion exchange chromatography.
Proteins were purified by affinity chromatography and gel filtration as described above . Flow cytometry.
Recombinant FR proteins were purified as described above for human FRa.
Proteins were purified by metal chelate affinity chromatography to greater than 90 % homogeneity.
All the corresponding proteins were purified by affinity chromatography on IMAC resin.
All proteins were purified by a two-step procedure, first using protein A chromatography.
The recombinant fusión proteins were purified to homogeneity on protein A sepharose.
Binding proteins were purified on a resin to which indol ligand 91 was covalently attached.
All recombinant proteins were purified by affinity chromatography and gel filtration.
Proteins were purified in 1 of 3 ways depending on the fusión partner and the protein 's solubility,.

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