3.4.21.9	synthesis	a huge number of therapeutic proteins such as antibodies, coagulation factors, growth hormones or vaccines are produced as fusion proteins. To obtain the therapeutic protein in its monomeric, active form, the fusion partner has to be removed either by chemical or enzymatic cleavage. Enterokinase is a very attractive tool for the in vitro cleavage of fusion proteins	707812	
3.4.21.9	analysis	cellular libraries of peptide substrates, CLiPS, are used to study substrate specificities, fluorescent reporter substrates on the surface of Escherichia coli as N-terminal conjugates are used as whole-cell protease activity assays	684000	
3.4.21.9	biotechnology	EK is immobilised on hexamethylamino Sepabeads or on amino-modified paramagnetic microspheres. 50% of activity remains after immobilisation	683266	
3.4.21.9	analysis	enteropeptidase activity is influenced by accessibility of the target site and by downstream sequences	683192	
3.4.21.9	biotechnology	enteropeptidase is a serine protease used in different biotechnological applications. For many applications the smaller light chain can be used to avoid the expression of the rather large holoenzyme	718352	
3.4.21.9	synthesis	gene engineering studies on processing fusion proteins	667758	
3.4.21.9	medicine	human TRAIL is a candidate for clinical application in cancer therapy, activity is lost in some forms of recombinant TRAIL, refolding of thioredoxin/TRAIL and cleavage by enteropeptidase yield a biological active anticancer agent	683279	
3.4.21.9	biotechnology	purification of 6.8 mg bioactive enzyme from 1l fermentation broth	683994	
3.4.21.9	biotechnology	study presents a simple and cost-effective procedure for a large-scale production	684030	
3.4.21.9	synthesis	the cleavage immediately after the carboxyl-terminal residue of the (Asp)4-Lys recognition sequence allows regeneration of native amino-terminal residues of recombinant proteins, e.g. removal of the thioredoxin and polyhistidine fusion partners from proteins of intrest	95583