Results 321 to 330 of about 665,350 (364)

Chitosan nanoparticles conjugate with trypsin and trypsin inhibitor

Carbohydrate Polymers, 2016
Chitosan-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, 2017
Al 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, Laurent Kreplak, P. Chanphai   +2 more
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Studies on Trypsin: I. The Anticoagulant Action of Trypsin

Gastroenterology, 1952
Summary 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, Irving Innerfield, James W. Benjamin   +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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Heat of reaction between trypsin and soybean trypsin inhibitor

Archives of Biochemistry and Biophysics, 1952
Abstract 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.
Julian M. Sturtevant, Alan Dobry
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A radioactive method for the measurement of trypsin and trypsin-like activities

Analytical Biochemistry, 1989
A simple and highly sensitive method for the assay of trypsin has been developed by making use of the phosphorylated synthetic peptide Leu-Arg-Arg-Ala-Ser-(32P)-Leu-Gly as substrate. The technique has been adapted from the phosphocellulose method of R. Roskoski, Jr. (in Methods in Enzymology (Corbin, J., and Hardman, J., Eds.), Vol. 99, pp.
Susana Passeron, P. Fernandez Murray, Maria Leonor Cantore, Susana Silberstein   +3 more
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TRYPSIN AND TRYPSIN INHIBITORS FROM PENAEID SHRIMP

Journal of Food Biochemistry, 2002
Trypsin inhibitors from four species of shrimp, P. vannamei, P. monodon, P. stylirostris, and P. californiensis were characterized by test tube and electrophoretic assays. Inhibitors in the four phylogenetically related species showed different inhibitory capacity and specificity for orthologous trypsins. Inhibitors from P.
Cristiane De Albuquerque-Cavalcanti, M. Angeles Navarrete del Toro, Fernando García-Carreño   +2 more
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Tumour-associated trypsin inhibitor and tumour-associated trypsin

Scandinavian Journal of Clinical and Laboratory Investigation, 1990
Tumour-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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Trypsin, for the defense

Nature Immunology, 2002
The α-defensins from Paneth cells in intestinal crypts need processing to be fully functional. Unlike for mice, the cleaving enzyme for human HD5 turns out to be trypsin.
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On the Potential Role of Trypsin and Trypsin Inhibitors in Acute Pancreatitis

1984
The 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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