Enterokinase
Enterokinase structure
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Common Name | Enterokinase | ||
|---|---|---|---|---|
| CAS Number | 9014-74-8 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
| Symbol |
GHS07, GHS08 |
Signal Word | Danger | |
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Molecular insights into the interaction between Plasmodium falciparum apical membrane antigen 1 and an invasion-inhibitory peptide.
PLoS ONE 9(10) , e109674, (2014) Apical membrane antigen 1 (AMA1) of the human malaria parasite Plasmodium falciparum has been implicated in invasion of the host erythrocyte. It interacts with malarial rhoptry neck (RON) proteins in the moving junction that forms between the host cell and th... |
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Improved insecticidal activity of a recombinant baculovirus expressing spider venom cyto-insectotoxin.
Appl. Microbiol. Biotechnol. 99 , 10261-9, (2015) Baculoviruses have a long history of safe use as specific, environmentally friendly insecticides that provide alternatives to chemical pesticides for controlling insect pests. However, their use has been limited by several factors, particularly their slow pat... |
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Pheromone binding proteins enhance the sensitivity of olfactory receptors to sex pheromones in Chilo suppressalis.
Sci. Rep. 5 , 13093, (2015) Sexual communication in moths offers a simplified scenario to model and investigate insect sensory perception. Both PBPs (pheromone-binding proteins) and PRs (pheromone receptors) are involved in the detection of sex pheromones, but the interplay between them... |
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Characterization of bioactive recombinant antimicrobial peptide parasin I fused with human lysozyme expressed in the yeast Pichia pastoris system.
Enzyme Microb. Technol. 77 , 61-7, (2015) Parasin I (PI) is a 19 amino acid peptide with potent antimicrobial activities against a broad spectrum of microorganisms and is a good candidate for development as a novel antimicrobial agent. The objective of this study was to express and characterize a cod... |
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IL-1 Receptor Antagonist Chimeric Protein: Context-Specific and Inflammation-Restricted Activation.
J. Immunol. 195 , 1705-12, (2015) Both IL-1α and IL-1β are highly inflammatory cytokines mediating a wide spectrum of diseases. A recombinant form of the naturally occurring IL-1R antagonist (IL-1Ra), which blocks IL-1R1, is broadly used to treat autoimmune and autoinflammatory diseases; howe... |
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Conserved C272/278 in b domain regulate the function of PDI-P5 to make lysozymes trypsin-resistant forms via significant intermolecular disulfide cross-linking.
Biochim. Biophys. Acta 1854(5) , 485-91, (2015) Protein disulfide isomerase-P5 (P5) is thought to have important functions as an oxidoreductase, however, molecular functions of P5 have not been fully elucidated. We have reported that P5 has insulin reductase activity and inhibits lysozyme refolding by form... |
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A fluorogenic method for measuring enteropeptidase activity: spectral shift in the emission of GD4K-conjugated 7-amino-4-methylcoumarin.
BMB Rep. 44(7) , 458-61, (2011) Enteropeptidase is a serine protease secreted by the pancreas and converts inactive trypsinogen to active trypsin. Enteropeptidase cleaves the C-terminal end of the substrate recognition sequence Asp-Asp-Asp-Asp-Lys (D(4)K). The assay for enteropeptidase has ... |
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In vitro activation and enzyme kinetic analysis of recombinant midgut serine proteases from the Dengue vector mosquito Aedes aegypti.
BMC Biochem. 12 , 43, (2011) The major Dengue virus vector Aedes aegypti requires nutrients obtained from blood meal proteins to complete the gonotrophic cycle. Although bioinformatic analyses of Ae. aegypti midgut serine proteases have provided evolutionary insights, very little is know... |
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New strategy for specific activation of recombinant microbial pro-transglutaminase by introducing an enterokinase cleavage site.
Biotechnol. Lett. 35(3) , 383-8, (2013) Recombinant microbial transglutaminase (rMTG) is usually expressed as a soluble zymogen (pro-rMTG) in heterologous expression systems but proteolytic activation of the inactive pro-rMTG is essential. Instead of screening proteases for activating pro-rMTG, we ... |
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Optimized soluble expression and purification of an aggregation-prone protein by fusion tag systems and on-column cleavage in Escherichia coli.
Protein Pept. Lett. 19(12) , 1324-9, (2012) Previously we constructed a fusion protein based on GLP-1 and globular adiponectin but unfortunately its yield was low because it was mainly expressed as inclusion bodies. Herein to optimize the soluble expression of this fusion protein we tried several fusio... |