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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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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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Phytochemistry, 1973
Abstract Trypsin inhibitors were found in several food plants. Potato and sweet corn were the most inhibitory, while fruits had negligible activity. Intermediate in activity were sweet potato, spinach, broccoli, Brussels sprouts and cucumber. The trypsin inhibitor of sweet corn was isolated by extraction in dilute salt solution, ammonium sulfate ...
H.L. Mitchell, Ingrid Chen
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Abstract Trypsin inhibitors were found in several food plants. Potato and sweet corn were the most inhibitory, while fruits had negligible activity. Intermediate in activity were sweet potato, spinach, broccoli, Brussels sprouts and cucumber. The trypsin inhibitor of sweet corn was isolated by extraction in dilute salt solution, ammonium sulfate ...
H.L. Mitchell, Ingrid Chen
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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.
Irene Mueller +8 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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Die Makromolekulare Chemie, 1960
AbstractThe optical rotatory properties, amino acid composition, chromatographic fractionation, and enzymic inhibition activity of several trypsin inhibitors were investigated. The homogeneity of these proteins was tested by free boundary electrophoresis and sedimentation in the ultracentrifuge.
T. Ikenaka +2 more
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AbstractThe optical rotatory properties, amino acid composition, chromatographic fractionation, and enzymic inhibition activity of several trypsin inhibitors were investigated. The homogeneity of these proteins was tested by free boundary electrophoresis and sedimentation in the ultracentrifuge.
T. Ikenaka +2 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.
Maria A. Juliano +3 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.
Julian M. Sturtevant, Alan Dobry
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Energy embedding of trypsin inhibitor
Biopolymers, 1982AbstractEnergy embedding has been shown recently to be a useful extension of the distance geometry approach to conformational calculations in the case of very small molecules and simple energy functions. This paper tests the ability of energy embedding to locate low energy conformations satisfying both weak and strong geometric constraints when the ...
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TRYPSIN AND TRYPSIN INHIBITORS FROM PENAEID SHRIMP
Journal of Food Biochemistry, 2002Trypsin 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 +2 more
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