Results 341 to 350 of about 736,972 (389)
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Biochemical and Biophysical Research Communications, 1982
Abstract The denaturation of α- and β-trypsin in alkaline and neutral solution was studied. The denaturation of α-trypsin was a strict second-order reaction at neutrality. However, the denaturation of β-trypsin was not a pure secondorder reaction at the same pH.
Myron L. Bender +2 more
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Abstract The denaturation of α- and β-trypsin in alkaline and neutral solution was studied. The denaturation of α-trypsin was a strict second-order reaction at neutrality. However, the denaturation of β-trypsin was not a pure secondorder reaction at the same pH.
Myron L. Bender +2 more
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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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Journal of Allergy, 1964
T rypsin (Parenzyme) is used extensively in the treatment of a variety of disorders.1-26 These conditions include thrombophlebitis, peripheral vascular disease, venous thrombosis, postoperative edema, traumatic swelling, hematomas, ulcerative lesions, postphlebitic syndrome, etc.
Leo H. Criep, Lewis R. Beam
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T rypsin (Parenzyme) is used extensively in the treatment of a variety of disorders.1-26 These conditions include thrombophlebitis, peripheral vascular disease, venous thrombosis, postoperative edema, traumatic swelling, hematomas, ulcerative lesions, postphlebitic syndrome, etc.
Leo H. Criep, Lewis R. Beam
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The Journal of Biochemistry, 1982
We devised a new separation technique for the protein, "affinophoresis," which is based on its specific affinity and utilizes electrophoresis. This technique requires a carrier macromolecule, "affinophore," which contains both an affinity ligand for a certain protein and many charges, either positive or negative, in order to migrate rapidly in an ...
Ken-ichi Kasai, Kiyohito Shimura
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We devised a new separation technique for the protein, "affinophoresis," which is based on its specific affinity and utilizes electrophoresis. This technique requires a carrier macromolecule, "affinophore," which contains both an affinity ligand for a certain protein and many charges, either positive or negative, in order to migrate rapidly in an ...
Ken-ichi Kasai, Kiyohito Shimura
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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
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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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