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Trypsinogen, Trypsin, Trypsin-Substrate and Trypsin-Inhibitor Complexes in Urea Solutions
European Journal of Biochemistry, 1968The denaturation in urea of trypsinogen, trypsin and trypsin derivatives is first-order with respect to protein. 1 Structural modifications affecting the trypsinogen molecule were detected by studying the influence of pH on the rate of denaturation. The acidification of trypsinogen leads to the appearance of 2 reversible equilibria I′⇌ II′⇌ III′
M, Delaage, M, Lazdunski
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Journal of Gastroenterology, 2006
Trypsin activity is properly suppressed in the pancreatic acinar cells under normal conditions. A small amount of trypsinogen is converted to active trypsin and inactivated by pancreatic secretory trypsin inhibitor (PSTI), thereby preventing damage to pancreatic acinar cells as a first line of defense.
Masahiko, Hirota +2 more
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Trypsin activity is properly suppressed in the pancreatic acinar cells under normal conditions. A small amount of trypsinogen is converted to active trypsin and inactivated by pancreatic secretory trypsin inhibitor (PSTI), thereby preventing damage to pancreatic acinar cells as a first line of defense.
Masahiko, Hirota +2 more
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Journal of the American Oil Chemists' Society, 2021
AbstractFor expressing trypsin inhibitor activity (TIA), trypsin units inhibited (TUI), trypsin inhibited, and trypsin inhibitors have been used. Although the last two units are preferred, their calculations in current practices require refinement.
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AbstractFor expressing trypsin inhibitor activity (TIA), trypsin units inhibited (TUI), trypsin inhibited, and trypsin inhibitors have been used. Although the last two units are preferred, their calculations in current practices require refinement.
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Heat of reaction between trypsin and soybean trypsin inhibitor
Archives of Biochemistry and Biophysics, 1952Abstract Calorimetric determinations of the heat of reaction between trypsin and soybean trypsin inhibitor protein indicate that ΔH for the reaction at 25 ° is 0 ± 1 kilocal./mole of trypsin reacted, if similar experiments with the inhibitor protein and bovine serum albumin are accepted as valid controls.
A, DOBRY, J M, STURTEVANT
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Interaction of Urinary Trypsin Inhibitor, UTI68, with Bovine Trypsin
The Journal of Biochemistry, 1982One molecule of UTI68, a trypsin inhibitor purified from urine of healthy men, inhibited four molecules of bovine trypsin. This finding suggests the formation of various complexes of UTI68 with 1 to 4 molecules of trypsin. However, SDS polyacrylamide gel electrophoresis of the reaction products of UTI68 with trypsin showed that, at molecular ratios of ...
M, Tominaga, H, Takeda, M, Muramatu
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Energy embedding of trypsin inhibitor
Biopolymers, 1982AbstractEnergy embedding has been shown recently to be a useful extension of the distance geometry approach to conformational calculations in the case of very small molecules and simple energy functions. This paper tests the ability of energy embedding to locate low energy conformations satisfying both weak and strong geometric constraints when the ...
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Trypsin, trypsinogen and trypsin inhibitor in human pancreatic juice
The American Journal of Medicine, 1960Abstract 1.1. Benzoylarginine-paranitroanilide was employed as substrate in a method which permits simple, sensitive and rapid assay of trypsin. 2.2. Human pancreatic juice obtained by catheter drainage of the duct of Wirsung exhibited no spontaneous tryptic activity.
B J, HAVERBACK +3 more
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Interrelation of the urinary trypsin inhibitor to human plasma inter-alpha-trypsin inhibitor
Clinical Biochemistry, 19731. Immunological investigations were conducted with specific antisera to the urinary trypsin inhibitor (UTI) and human plasma trypsin inhibitors. The results indicated that UTI is not interrelated to either α 1 -anti-trypsin or α 2 -macroglobulin, the main plasma trypsin inhibitors. UTI appears to be interrelated with inter- α -trypsin inhibitor (
G J, Proksch, J, Lane, C D, Nordschow
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Sunflower trypsin inhibitor‐1, proteolytic studies on a trypsin inhibitor peptide and its analogs
Peptide Science, 2010AbstractSunflower trypsin inhibitor‐1 (SFTI‐1) is a 14 amino acid cyclic peptide from sunflower seeds, which possesses exceptionally potent trypsin‐inhibitory activity, and has promise as a stable peptide‐based drug template. Within its compact structure, SFTI‐1 combines a head‐to‐tail cyclized backbone and a disulfide bond.
Colgrave, Michelle +4 more
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On the Potential Role of Trypsin and Trypsin Inhibitors in Acute Pancreatitis
1984The protective role of alpha 2-macroglobulin, alpha 1-antitrypsin and Aprotinin against trypsin-induced effects on C3 and kininogen was studied in a human in vitro model. When human cationic trypsin was added to human serum or plasma, there was a gradual saturation of alpha 2-macroglobulin and later of alpha 1-antitrypsin.
A, Lasson, K, Ohlsson
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