A recombinant Pichia pastoris containing enterokinase light chain gene from bovine was cultured in flasks firstly at different pH, methanol addition, and cell mass concentration for enterokinase production. Activity of enterokinase increased as cell mass concentration increased at more than = 6 % methanol added. No significant change of activity of enterokinase was observed when methanol added ...

Mucosal enterokinase activity was established at intervals throughout the small intestine in guinea-pigs; maximum activity was present in the duodenum and proximal jejunum in new born as well as adult animals. Transposition of 5 cm lengths of small gut from the high enterokinase containing proximal region to the distal intestine and vice versa showed that mucosal enterokinase activity in the tr...

THE effect of heat upon the properties of enterokinase has not been studied in very great detail, and the work that has been done is not of a quantitative nature. Mellanby and Woolley [1913] stated that enterokinase is destroyed in 5 mins. at 650, and is immediately inactivated in the presence of free acid. In more recent work Waldschmidt-Leitz [1924, 1925] has shown that enterokinase solutions...

Enterokinase is a protease of the intestinal brush border that specifically cleaves the acidic propeptide from trypsinogen to yield active trypsin. This cleavage initiates a cascade of proteolytic reactions leading to the activation of many pancreatic zymogens. The full-length cDNA sequence for bovine enterokinase and partial cDNA sequence for human enterokinase were determined. The deduced ami...

Enterokinase (enteropeptidase) is expressed only in proximal small intestine, where it initiates digestive enzyme activation by converting trypsinogen into trypsin. To investigate this restricted expression pattern, mouse enterokinase cDNA was cloned, and the distribution of enterokinase mRNA and enzymatic activity were determined in adult mice and during gestation. Analysis of enterokinase seq...

Bovine enterokinase was purified from duodenal mucosa. The purification included an initial extraction with 2% deoxycholate, ammonium sulfate fractionations, DEAE-cellulose chromatography, and affinity chromatography on basic pancreatic trypsin inhibitor (Kunitz) (PTI)-Sepharose. The purified enzyme contained 35% carbohydrate; it had a molecular weight of 150,000, with a heavy (115,000) and lig...

Crystalline trypsinogen is most readily and completely transformed into trypsin by means of enterokinase in the range of pH 5.2-6.0 at 5 degrees C. and at a concentration of trypsinogen of not more than 0.1 mg. per ml. The action of enterokinase under these conditions is that of a typical enzyme. The process follows closely the course of a catalytic unimolecular reaction, the rate of formation ...

Enterokinase (enteropeptidase) is a heterodimeric serine protease that is responsible for the physiological activation of trypsinogen by highly specific cleavage of the trypsinogen activation peptide following the sequence (Asp)4-Lys. In this paper, we report the cloning and functional expression of a cDNA encoding the catalytic domain (light chain) of bovine enterokinase. The nucleotide sequen...

Enterokinase was measured in peroral intestinal biopsies showing normal histology and in those from untreated coeliac patients which showed gross villous atrophy. There was no significant difference in the specific activity of enterokinase between these two groups. These results do not support the recent hypothesis that enterokinase is a brush border enzyme, but would be consistent with the ide...

The distribution of enterokinase in human intestine was studied in operative mucosal biopsies using specific antiserum to human enterokinase, previously purified to apparent homogeneity by affinity chromatography and immunoabsorption. Fluorescence was observed in the brush-border and glycocalyx of the duodenum and proximal 15 cm of jejunum distal to the D/J flexure. Distal jejunum and ileum as ...