Results 261 to 270 of about 367,770 (313)
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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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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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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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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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Naturally Occurring Trypsin Inhibitors
1954Publisher Summary This chapter discusses the following naturally occurring trypsin inhibitors: (1) pancreatic inhibitor of Kunitz and Northrop, (2) a second inhibitor from pancreas crystallized by Kazal, Spicer, and Brahinsky, (3) soybean inhibitor, (4) colostrum inhibitor, (5) lima bean inhibitor, (6) ovomucoid, (7) blood plasma inhibitor, and (8 ...
M, LASKOWSKI, M, LASKOWSKI
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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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