Results 211 to 220 of about 424,136 (259)
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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 ...
K, Shimura, K, Kasai
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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 ...
K, Shimura, K, Kasai
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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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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.
H L, Wu, C, Kundrot, M L, Bender
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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.
H L, Wu, C, Kundrot, M L, Bender
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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.
F D, WHITE, J M, BOWMAN
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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.
F D, WHITE, J M, BOWMAN
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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 ...
P, Chanphai +2 more
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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 ...
P, Chanphai, H A, Tajmir-Riahi
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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
I, INNERFIELD, A, ANGRIST, J W, BENJAMIN
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Trypsin Uptake and Trypsin-Inhibitor Complexes
Biology of the Neonate, 2009Previous studies have suggested that both newborn animals and humans absorb intact proteases from the intestine in greater amounts than do adults. Absorbed proteases are rapidly complexed in plasma by several inhibitors which inactivate free proteases. In order to confirm increased intestinal uptake in newborns, we evaluated the plasma trypsin activity
Jeremiah J. Levine +3 more
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