Results 161 to 170 of about 153,765 (211)
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Archives of Biochemistry and Biophysics, 1974
Abstract Fetuin per se is a moderately strong trypsin inhibitor of the temporary type and retains its antitryptic activity upon desialicization. It forms a reversible 1:1 complex with β-trypsin and is functionally homogeneous in this respect. Complex formation is an entropy-driven reaction evidently due to release of structured water associated ...
F, Galembeck, J R, Cann
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Abstract Fetuin per se is a moderately strong trypsin inhibitor of the temporary type and retains its antitryptic activity upon desialicization. It forms a reversible 1:1 complex with β-trypsin and is functionally homogeneous in this respect. Complex formation is an entropy-driven reaction evidently due to release of structured water associated ...
F, Galembeck, J R, Cann
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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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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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Trypsin Uptake and Trypsin-Inhibitor Complexes
Neonatology, 1989Previous 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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Trypsin inhibitors for the treatment of pancreatitis
Bioorganic & Medicinal Chemistry Letters, 2016Proline-based trypsin inhibitors occupying the S1-S2-S1' region were identified by an HTS screening campaign. It was discovered that truncation of the P1' moiety and appropriate extension into the S4 region led to highly potent trypsin inhibitors with excellent selectivity against related serine proteases and a favorable hERG profile.
Trixi, Brandl +8 more
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Coevolution of insect trypsins and inhibitors
Archives of Insect Biochemistry and Physiology, 2004AbstractMany plant proteinase inhibitors have lysine at the P1 position, presumably to avoid hydrolysis by insect trypsins. Lepidopteran trypsins appear to have adapted to resist proteinase inhibitors through increased inhibitor hydrolysis and decreased binding to inhibitor hydrophilic reactive sites.
A R, Lopes +3 more
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Current Protein & Peptide Science, 2004
SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar K(i) value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors.
Korsinczky, M. L. J. +2 more
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SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar K(i) value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors.
Korsinczky, M. L. J. +2 more
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Heat of reaction between trypsin and soybean trypsin inhibitor
Archives of Biochemistry and Biophysics, 1952Abstract 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.
A, DOBRY, J M, STURTEVANT
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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.
Masahiko, Hirota +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.
Masahiko, Hirota +2 more
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Journal of the American Oil Chemists' Society, 2021
AbstractFor expressing trypsin inhibitor activity (TIA), trypsin units inhibited (TUI), trypsin inhibited, and trypsin inhibitors have been used. Although the last two units are preferred, their calculations in current practices require refinement.
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AbstractFor expressing trypsin inhibitor activity (TIA), trypsin units inhibited (TUI), trypsin inhibited, and trypsin inhibitors have been used. Although the last two units are preferred, their calculations in current practices require refinement.
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