Examples of 'enterokinase' in a sentence
Meaning of "enterokinase"
enterokinase (noun) - an enzyme produced in the small intestine that plays a crucial role in the digestion of proteins by converting trypsinogen into its active form, trypsin
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- An enzyme, secreted by the upper intestinal mucosa, that catalyzes the activation of trypsinogen by converting it to trypsin
How to use "enterokinase" in a sentence
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enterokinase
Compositions and methods of producing enterokinase in yeast.
An enterokinase recognition site is indicated by an arrow.
The arrow indicates the cleavage site of the enterokinase.
Various enterokinase cleavage sites are known in the art.
A parallel set of samples received no enterokinase but underwent similar incubation.
Aspects of the present specification disclose polynucleotide molecules encoding enterokinase.
Assays for enterokinase activity.
The presence of the reducing agent allows to optimize enterokinase cleavage.
The histidine linker is removed by enterokinase cleavage after purification is complete.
The enterokinase light chain contains the catalytic activity and is sufficient for cleavage.
Pavlov named it enterokinase.
After the Trx fusión there exists protease cleavage sites for thrombin and enterokinase.
The vector also contains an enterokinase cleavage site right before the protein of interest.
In a preferred embodiment, the protease cleavage site is an enterokinase site.
The propeptide is removed by enterokinase cleavage, leading to the formation of active mesotrypsin.
See also
The collagen is cleaved from the 6 histidine tag with enterokinase.
Uncleaved fusión protein, thioredoxin and enterokinase remained bound on the column.
The method of claim 1 wherein the capture protein is a modified enterokinase.
The third construct had an enterokinase cleavage site, instead of the thrombin cleavage site.
Aspects of the present specification provide, in part, a polynucleotide molecule encoding enterokinase.
Trypsinogen is activated via the duodenal enzyme enterokinase into its active form trypsin.
The poly-histidine tag can be removed by digestion with the protease enterokinase.
The electrophoretic migration indicates that the enterokinase has undergone post-translational modification.
Enterokinase is one example of an enzyme ( serine protease ) that cleaves a specific amino acid sequence.
They are also indicated in cases of mucoviscidose and lipase, colipase and enterokinase deficiencies.
Enterokinase is one example of an enzyme ( serine protease ) that cut a specific amino acid sequence.
After purification, the fusión proteins were submitted to enterokinase cleavage permitting the release of calcitonin.
By enterokinase or by Factor Xa, or by the chemical methods known in the art.
Activation of trypsinogen = = Trypsinogen is activated by enteropeptidase also called enterokinase.
The signal peptidase 1 and the enterokinase cleavage site in the are underlined with a broken line.
Examples of such proteases include thrombin, enterokinase and factor Xa.
A C-terminus enterokinase recognition site allows for cleavage of these tags.
Analogous cleavage experiments were done also with enterokinase ( Sigma ) and calpain.
Another non-limiting example of Enterokinase is the light chain alone which comprises the catalytic domain.
Cleavage in vitro of the hybrid polypeptide produced in E. coli cells by the enzyme enterokinase.
In further aspects, a polynucleotide molecule encoding enterokinase may be a polynucleotide variant disclosed in Table 2.
This construct contains the linker sequence, from which GRF is released by enterokinase digestion.
Enterokinase was inactivated by adding 1 × EDTA-free complete protease inhibitor tablet.
A library of claim 5, wherein the recognition site is the site for enterokinase or Factor Xa.
This sequence has an enterokinase cleavage site after the first lysine residue ( amino acid 7 ).
Proteolytic enzymes for such cleavage and their recognition sequences include Factor Xa, thrombin and enterokinase.
An enterokinase ( EK ) cleavage-site was inserted for cleavage of the tag.
Examples of such include cyanogens bromide, trypsin, enterokinase and Factor Xa.
The enterokinase was then removed with the EK-Away system ( Invitrogen ) according to the manufacturers recommendation.
Proteases such as trypsin, Acromobacter lyticus protease and Enterokinase may be used.
Enterokinase cleaves after lysine in the sequence Asp-Asp-Asp-Asp-Lys.
Figure 6B illustrates the HPLC chromatogram of the peptide of Figure 6A after cleavage by enterokinase.
Examples of making a polynucleotide molecule encoding enterokinase are described in Examples 1, 2, and 4-6.
The method of embodiment 44, wherein the method further comprises purifying the enterokinase.
CS are the enterokinase cleavage site ( EK ) and the FXa cleavage site ( FXa ).
