Results 261 to 270 of about 259,629 (307)

Influence of the lysosomal elastase inhibitor eglin on development of interstitial lung edema in E. coli bacteremia in pigs [PDF]

open access: yes, 1987
Jochum, Marianne   +5 more
core  

<i>Clostridium perfringens</i> type C-associated emphysematous gastritis in a dog with pancreatic disease. [PDF]

open access: yesJ Vet Diagn Invest
Shekelle KL   +5 more
europepmc   +1 more source

Metabolic engineering of soybean for improving grain quality for animal consumption. [PDF]

open access: yesFront Plant Sci
Kafer JM   +7 more
europepmc   +1 more source

Serine protease-driven entry and S2 ' cleavage flexibility of feline coronavirus during feline enterocyte infections. [PDF]

open access: yesPLoS Pathog
Chen B   +5 more
europepmc   +1 more source

Gene expression and evolution of Bowman-Birk protease inhibitors in wild and domesticated <i>Vigna</i> (Fabaceae) species. [PDF]

open access: yesFront Plant Sci
Toini E   +10 more
europepmc   +1 more source
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Trypsin Inhibitor Assay: Expressing, Calculating, and Standardizing Inhibitor Activity in Absolute Amounts of Trypsin Inhibited or Trypsin Inhibitors

JAOCS, 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.
Keshun Liu
exaly   +2 more sources

Fetuin as a trypsin inhibitor

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
openaire   +2 more sources

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 ...
P, Chanphai   +2 more
openaire   +2 more sources

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