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trypsin

Definitions

  • WordNet 3.6
    • n trypsin an enzyme of pancreatic origin; catalyzes the hydrolysis of proteins to smaller polypeptide units
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Webster's Revised Unabridged Dictionary
    • n Trypsin (physiol) A proteolytic enzyme present in the pancreatic juice. Unlike the pepsin of the gastric juice, it acts in a neutral or alkaline fluid, and not only converts the albuminous matter of the food into soluble peptones, but also, in part, into leucin and tyrosin.
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Century Dictionary and Cyclopedia
    • n trypsin The proteolytic ferment which is the active principle of the pancreatic fluid; pancreatine. It is active in neutral or alkaline solutions, and not only produces peptones from the proteid matter of the food, but further converts a portion of the peptones into leucin and tyrosin.
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Chambers's Twentieth Century Dictionary
    • n Trypsin trip′sin a ferment which occurs in the secretion of the pancreas, and may be isolated from the pancreatic juice, as pepsin from the gastric
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Etymology

Webster's Revised Unabridged Dictionary
Gr. a rubbing, fr. to rub, grind. So called because it causes protein to break up or to fall apart
Chambers's Twentieth Century Dictionary
Gr., from tribein, to rub, the substance having been first found on rubbing down the pancreas with glycerine.

Usage

In literature:

Why, there was my theory of the hydrolysis of casein by trypsin, which Professor Walters had been carrying out in his laboratory.
"The Jacket (The Star-Rover)" by Jack London
This is because the pancreatic ferment (trypsin) has digested the casein into "peptone," which does not curdle.
"A Practical Physiology" by Albert F. Blaisdell
One of the most recent is treatment by trypsin, a pancreatic ferment.
"Encyclopaedia Britannica, 11th Edition, Volume 5, Slice 2" by Various
This phenomenon has been studied in connection with the zymogens of the digestive proteases, pepsin and trypsin.
"The Chemistry of Plant Life" by Roscoe Wilfred Thatcher
It is digested by trypsin and slowly destroyed by the fat solvent anaesthetics, such as chloroform.
"The Nature of Animal Light" by E. Newton Harvey
These unorganized ferments are such as rennin, pepsin, trypsin, ptyalin.
"The Book of Cheese" by Charles Thom and Walter Warner Fisk
SHAKLEE, A. O., and MELTZER, S. J.: (2) The Influence of Shaking upon Trypsin and Rennin, etc., Proceed.
"Scurvy Past and Present" by Alfred Fabian Hess
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In news:

An in-depth characterization of maize- derived trypsin revealed an unusual nonconsensus N-linked glycosylation.
An in-depth characterization of maize-derived trypsin revealed an unusual nonconsensus N-linked glycosylation.
Earth Spring Foods recently launched PrimaSoy, an all-natural, patented process for deactivating estrogen, phytic acid, oligosaccharides and trypsin inhibitors in soy .
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In science:

Preparatory to an LC-MS/MS experiment, a protein sample is digested using trypsin or other proteolytic enzyme.
Analyzing LC-MS/MS data by spectral count and ion abundance: two case studies
In the simplest case, the species is one of the amino acid sequences generated by an in silico digest of the protein database, e.g., by trypsin.
Analyzing LC-MS/MS data by spectral count and ion abundance: two case studies
To mimic biological replicates, Kolker et al. prepared six (6) replicate samples of Mix1 and Mix 2 and digested each independently with trypsin.
Analyzing LC-MS/MS data by spectral count and ion abundance: two case studies
We believe this fact reflects a difference in the way in which the samples themselves were prepared; a contaminating (non-trypsin) proteolytic enzyme may have been introduced into the Mix 1 samples, or may have been more active in these than in the Mix 2 samples.
Analyzing LC-MS/MS data by spectral count and ion abundance: two case studies
We analzyed a subset of the data collected for the CPTAC study, comparing the trypsin-digested yeast protein lysate samples, designated QC2, with the UPS1 spike-in samples, designated A, B, C, D and E.
Analyzing LC-MS/MS data by spectral count and ion abundance: two case studies
Harmonic dynamics of proteins: normal modes and fluctuations in bovine pancreatic trypsin inhibitor.
Protein structural variation in computational models and crystallographic data
Our use of multiple protein structures brings out a previously unnoticed peculiarity in the rigidity of trypsin.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
The presence of a BPTI structure in the initial dataset let us to include a set of trypsins.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
The presence of a trypsin inhibitor, BPTI, in the Hespenheide dataset suggested to us that we should include trypsin itself in our study.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
The trypsins display a unique feature in their rigidity-dilution behaviour which sets them aside from any of our other proteins, as shown in Figure 10.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
Trypsin is the largest of the proteins in our set, typical structures having about 220 residues.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
Inspection of the RCD plots, however, shows that trypsin does not appear very different to other proteins in our set and does not divide into a larger number of sizeable rigid clusters.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
The distinctiveness of the trypsins is only evident because of our strategy of comparing multiple related structures from different organisms and conditions. A single trypsin structure might not have appeared unusual when compared against single examples of other proteins.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
Figure 10. A graph of hydrogen bond energy cutoff E versus rigidity for a wide variety of trypsin structures.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
Notice, in contrast to previous figures, that all trypsins lose rigidity for cutoffs in the region of -1 to -2 kcal/mol.
Sensitivity of protein rigidity analysis to small structural variations: a large-scale comparative analysis
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