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Naturally Occurring Trypsin Inhibitors
1954Publisher Summary This chapter discusses the following naturally occurring trypsin inhibitors: (1) pancreatic inhibitor of Kunitz and Northrop, (2) a second inhibitor from pancreas crystallized by Kazal, Spicer, and Brahinsky, (3) soybean inhibitor, (4) colostrum inhibitor, (5) lima bean inhibitor, (6) ovomucoid, (7) blood plasma inhibitor, and (8 ...
M, LASKOWSKI, M, LASKOWSKI
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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.
Masaki Ohmuraya +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.
Masaki Ohmuraya +2 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 (
C.D. Nordschow, J. Lane, G.J. Proksch
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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 ...
Mutumi Muramatu +2 more
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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.
Bernard J. Haverback +3 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.
Åke Lasson, Kjell Ohlsson
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Tumour-associated trypsin inhibitor and tumour-associated trypsin
Scandinavian Journal of Clinical and Laboratory Investigation, 1990Tumour-associated trypsin inhibitor (TATI) is a 6 kDa peptide, which is synthesized at low concentrations by several tumours and cell lines. Very high concentrations of TATI occur in mucinous ovarian tumours. Elevated levels of TATI occur in serum and urine in connection with most types of cancer at advanced stages. In mucinous ovarian cancer up to 85%
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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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Biochemistry, 1987
Hydrogen exchange rates of six beta-sheet peptide amide protons in bovine pancreatic trypsin inhibitor (BPTI) have been measured in free BPTI and in the complexes trypsinogen-BPTI, trypsinogen-Ile-Val-BPTI, bovine trypsin-BPTI, and porcine trypsin-BPTI. Exchange rates in the complexes are slower for Ile-18, Arg-20, Gln-31, Phe-33, Tyr-35, and Phe-45 NH,
Clare Woodward, Pamela Brandt
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Hydrogen exchange rates of six beta-sheet peptide amide protons in bovine pancreatic trypsin inhibitor (BPTI) have been measured in free BPTI and in the complexes trypsinogen-BPTI, trypsinogen-Ile-Val-BPTI, bovine trypsin-BPTI, and porcine trypsin-BPTI. Exchange rates in the complexes are slower for Ile-18, Arg-20, Gln-31, Phe-33, Tyr-35, and Phe-45 NH,
Clare Woodward, Pamela Brandt
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Nature, 1964
Urinary Trypsin Inhibitor (Mingin): Transformation into a New Trypsin Inhibitor by Acid Hydrolysis or by ...
Uwe Nissen, Tage Astrup
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Urinary Trypsin Inhibitor (Mingin): Transformation into a New Trypsin Inhibitor by Acid Hydrolysis or by ...
Uwe Nissen, Tage Astrup
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