Results 141 to 150 of about 8,341 (178)
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Oscillations of trypsinogen activation
Cryobiology, 1986Trypsin activity oscillations are shown by the autocatalytic activation of trypsinogen at 0 degrees C in aqueous solution. The oscillations were observed for 3-4 days and show only slight decrease in enzyme activity. The zymogen has been kept at ice water temperature and pH 8.2 in the presence of Mn2+ ion.
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Trypsinogen deficiency disease
The Journal of Pediatrics, 1964An infant with severe growth failure, hypoproteinemia, and edema is described. Clinical and laboratory studies indicate that this disorder results from an impaired capacity to hydrolyze ingested protein. By means of specific pancreatic proteolytic enzyme assays, it was established that the primary defect is a complete absence of trypsinogen. Absence of
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Unfolding Kinetics of Bovine Trypsinogen
European Journal of Biochemistry, 1996The unfolding kinetics of bovine trypsinogen were studied by a fluorescence‐detected stopped‐flow technique at pH 5.8. Trypsinogen unfolding appeared to be a rather complex reaction. Two phases, fast (with a time constant in the millisecond range) and slow, were detected in the range 2–7 M guanidium chloride (GdmC1).
J, Otlewski +3 more
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On bovine and porcine anionic trypsinogens
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1974Abstract The proportions of the anionic trypsinogens in cattle and pig pancreas do not exceed 10% of those of the well known cationic forms. Their amino acid compositions differ markedly, suggesting a relatively low degree of homology between both classes.
M N, Louvard, A, Puigserver
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Phylogeny of trypsinogen activation peptides
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1972Abstract 1. 1. Trypsinogen has been isolated and purified from several artiodactyls, including the sheep, the goat, the wild boar, the red deer, the roe deer and the dromedary. 2. 2. The activation peptides have been identified and their sequence determined. 3. 3.
S, Bricteux-Grégoire +2 more
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Trypsinogen-kinase fromAspergillus fumigatus
Experientia, 1980The activation of bovine trypsinogen by an extracellular acid proteinase from A. fumigatus is described. The enzyme activates trypsinogen optimally at pH 3.5 and 32 degrees C. The effect of substrate and enzyme concentrations on the activation has been studied and the Km-value has been determined.
M, Panneerselvan, S C, Dhar
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Serum trypsinogen in diagnosis of chronic pancreatitis
Digestive Diseases and Sciences, 1984A new radioimmunoassay to serum trypsinogen (Cis Trypsik) was tested in several patient populations. A low serum trypsinogen level (less than 10 ng/ml) was found in 69.2% of 13 patients with chronic pancreatic insufficiency (CPI), in 100% of 10 patients with 95-100% pancreatectomy but only in 14% of 14 patients with cancer of the pancreas.
W M, Steinberg, K K, Anderson
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1955
Publisher Summary Trypsin and trypsinogen were obtained in crystalline form from beef pancreas. Further work has improved methods of preparation and established that the transformation of trypsinogen into trypsin is a proteolytic process and may be accomplished either b y autocatalysis or by enterokinase, or by the kinase from a mold of the genus ...
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Publisher Summary Trypsin and trypsinogen were obtained in crystalline form from beef pancreas. Further work has improved methods of preparation and established that the transformation of trypsinogen into trypsin is a proteolytic process and may be accomplished either b y autocatalysis or by enterokinase, or by the kinase from a mold of the genus ...
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