Results 371 to 380 of about 712,349 (416)
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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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Food & Function, 2019
The molecular mechanism of the interaction between resveratrol and trypsin was studied using fluorescence spectroscopy (intrinsic fluorescence, synchronous fluorescence, three-dimensional fluorescence), ultraviolet-visible (UV-vis) spectroscopy, Fourier ...
Guoyan Ren +5 more
semanticscholar +1 more source
The molecular mechanism of the interaction between resveratrol and trypsin was studied using fluorescence spectroscopy (intrinsic fluorescence, synchronous fluorescence, three-dimensional fluorescence), ultraviolet-visible (UV-vis) spectroscopy, Fourier ...
Guoyan Ren +5 more
semanticscholar +1 more source
Journal of Chemical Education, 1977
Adaptation of an experiment entitled "The Turnover Number of Trypsin and Chymotrypsin" to illustrate the difference in basing enzyme concentration on weight, absorbance, or active sites; and that the method chosen to express enzyme concentration determines the calculated value of specific, molecular, and catalytic center activity.
Tom Holzman, Salvatore F. Russo
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Adaptation of an experiment entitled "The Turnover Number of Trypsin and Chymotrypsin" to illustrate the difference in basing enzyme concentration on weight, absorbance, or active sites; and that the method chosen to express enzyme concentration determines the calculated value of specific, molecular, and catalytic center activity.
Tom Holzman, Salvatore F. Russo
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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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Canadian Journal of Research, 1947
Details are given of a colorimetric method for the estimation of trypsin that can be utilized for the evaluation of the proteolytic activity of pancreatic secretion. Being an adaptation of a method that has been used successfully in a clinical laboratory for many years, it is suitable for routine clinical use.
J. M. Bowman, F. D. White
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Details are given of a colorimetric method for the estimation of trypsin that can be utilized for the evaluation of the proteolytic activity of pancreatic secretion. Being an adaptation of a method that has been used successfully in a clinical laboratory for many years, it is suitable for routine clinical use.
J. M. Bowman, F. D. White
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Chitosan nanoparticles conjugate with trypsin and trypsin inhibitor
Carbohydrate Polymers, 2016Chitosan-protein conjugates are widely used in therapeutic drug delivery. We report the bindings of chitosan nanoparticles with trypsin (try) and trypsin inhibitor (tryi), using thermodynamic analysis and multiple spectroscopic methods. Thermodynamic parameters ΔS, ΔH and ΔG showed chitosan-protein bindings occur mainly via H-bonding and van der Waals ...
H.A. Tajmir-Riahi, P. Chanphai
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Aggregation of trypsin and trypsin inhibitor by Al cation
Journal of Photochemistry and Photobiology B: Biology, 2017Al cation may trigger protein structural changes such as aggregation and fibrillation, causing neurodegenerative diseases. We report the effect of Al cation on the solution structures of trypsin (try) and trypsin inhibitor (tryi), using thermodynamic analysis, UV-Visible, Fourier transform infrared (FTIR) spectroscopic methods and atomic force ...
H.A. Tajmir-Riahi +2 more
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ACS Applied Materials and Interfaces, 2017
We describe the application of a fluorescently labeled water-soluble core-shell molecularly imprinted polymer (MIP) for fluorescence immunoassay (FIA) to detect trypsin. p-Aminobenzamidine (PAB), a competitive inhibitor of trypsin, was immobilized in the
Jingjing Xu, K. Haupt, B. Tse Sum Bui
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We describe the application of a fluorescently labeled water-soluble core-shell molecularly imprinted polymer (MIP) for fluorescence immunoassay (FIA) to detect trypsin. p-Aminobenzamidine (PAB), a competitive inhibitor of trypsin, was immobilized in the
Jingjing Xu, K. Haupt, B. Tse Sum Bui
semanticscholar +1 more source
Studies on Trypsin: I. The Anticoagulant Action of Trypsin
Gastroenterology, 1952Summary 1. Intravenous injection of large doses of trypsin given rapidly to dogs is romptly followed by a marked prolongation in clotting time and a depression in Ac-globulin concentration, plasma antithrombin, fibrinogen and prothrombin levels. 2. Antithrombin levels are initially depressed for 18 hours, followed by a secondary rise in titer lasting
Alfred Angrist +2 more
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Electrophoretic Heterogeneity of Trypsin [PDF]
Nature, 1959 IN a previous communication1 it was reported that crystalline trypsin, when submitted to paper electrophoresis at pH 2.6, shows the presence of three different and proteolitically active fractions, even in the absence of calcium ions.
L. V. Disitzer, A. Iachan, J. C. Perrone
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