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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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Biochemistry, 1987
Hydrogen exchange rates of six beta-sheet peptide amide protons in bovine pancreatic trypsin inhibitor (BPTI) have been measured in free BPTI and in the complexes trypsinogen-BPTI, trypsinogen-Ile-Val-BPTI, bovine trypsin-BPTI, and porcine trypsin-BPTI. Exchange rates in the complexes are slower for Ile-18, Arg-20, Gln-31, Phe-33, Tyr-35, and Phe-45 NH,
P, Brandt, C, Woodward
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Hydrogen exchange rates of six beta-sheet peptide amide protons in bovine pancreatic trypsin inhibitor (BPTI) have been measured in free BPTI and in the complexes trypsinogen-BPTI, trypsinogen-Ile-Val-BPTI, bovine trypsin-BPTI, and porcine trypsin-BPTI. Exchange rates in the complexes are slower for Ile-18, Arg-20, Gln-31, Phe-33, Tyr-35, and Phe-45 NH,
P, Brandt, C, Woodward
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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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Tumour-associated trypsin inhibitor and tumour-associated trypsin
Scandinavian Journal of Clinical and Laboratory Investigation, 1990Tumour-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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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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Interactions between trypsin, α2 macroglobulin and soybean trypsin inhibitor
Biochemical and Biophysical Research Communications, 1973Abstract The present study reveals that a trypsin- α 2 macroglobulin complex cannot be dissociated by the intervention of soybean trypsin inhibitor even after a 60 hour-incubation time. If the inhibitor is first bound to trypsin, the addition of α 2 macroglobulin restores about 60% of the enzyme activity.
G, Krebs, Y, Jacquot-Armand
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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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