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Protein Trypsin

Trypsin (Section 27 10) A digestive enzyme that catalyzes the hydrolysis of proteins Trypsin selectively catalyzes the cleavage of the peptide bond between the carboxyl group of lysine or arginine and some other amino acid... [Pg.1296]

In the complex of the protein BPT1 with the protein trypsin, a close approximation to a tetrahedral adduct has been observed34 in the X-ray structure. This adduct is formed by addition of the reactive serine (ser... [Pg.87]

Transfer capillary, glass chip EOF ESI-ITMS Tryptic digest of horse apomyoglobin (7.4 nM), yeast proteins Trypsin Non-chip gradient frontal CEC separation C18 column 803... [Pg.240]

Digestion of proteins Trypsin Monolithic capillary column [348]... [Pg.187]

As one last example in this section, we plot in Figure 8 CPL and total emission spectra for Tb(III) as a substitutional replacement for Ca(II) in the protein trypsin [49]. The spectral region displayed in this figure corresponds to the 5D4 -4 Fg transition of Tb(III). CPL from Tb(III) and Eu(III) have been used to probe... [Pg.231]

It will be noted that the two proteins, trypsin inhibitor and lipoxidase, are apparently influenced differently by the microwave treatment. While microwave heating is more effective than hot water in destroying trypsin inhibitors (Table II) the reverse is true for lipoxidases(Table III). [Pg.155]

Lemer. J., Lami. H. Electronic energy tranrfer in some class B proteins trypsin, lysozyme, a-chymotrypsin and chymotrypsin A. In Exdted States of Biological Motecules. Birks, J. B. (Ed.) p. 601, London - New York - Toronto — Sydney Wiley 1976 Lombardi, J. R-, Daffotn, G. A J. Qiem. Phys. 44, 3882... [Pg.164]

C. Application Topographical Analysis of the Molecular Surfaces of the Proteins Trypsin and Trypsinogen... [Pg.238]

Pancreatic juice contains an alkaline fluid and enzymes, both of which empty into the duodenum. The alkaline pH contributes to neutralization of the acid that empties from the stomach. The enzymes amylase, lipase, trypsin, and chymotrypsin play major roles in the digestion of carbohydrates, fats, and proteins. Trypsin and chymotrypsin are secreted as inactive precursors and are converted to the active forms enzymatically. [Pg.24]

Isolated protein Trypsin digestion Peptides separated by MS... [Pg.311]

We have used the refined crystal structure of a small protein (trypsin inhibitor) as a system on which to test methods of analysis of solvent structure near protein surfaces in terms of 6-12 and electrostatic potentials. [Pg.213]

Wang and Johnson (2001) reported on test measurement methods that were major indicators of soybean oil quality. These tests included peroxide value, anisidine value, FFA content, phospholipid content, total tocopherol content, oxidative stability index, color, and moisture content. For soybean meal, they reported on urease activity, protein dispersibility index (PDI), rumen bypass or rumen undegradable protein, trypsin inhibitor activity, moisture content, residual oil content, protein content, fiber content, color, amino acid profiles, and protein solubility under alkaline (KOH) conditions. [Pg.193]

Hydrolysis of whey proteins (trypsin, chymotrypsin) Polysulfone UF membrane Production of peptides for medical use... [Pg.234]

Proteins Trypsin A reactor bed for immobilized trypsin in combination with a separation channel Electrospray ionization mass spectroscopy... [Pg.2451]

In 1998 Ruaan et al su ested methacrylic block copolymers similar to the ones proposed by Patrickios as protein displacers in hydrophobic interaction chromatography on octyl-sepharose. The molecular masses of the displacer were relatively small (between 3000 and 4000 g/mol). When the isotherms were recorded, the displacer isotherms were below the protein (trypsin, a-chymotrypsin) isotherms (Fig. 4.7). According to the conventional formalism, this would mean that the triblock polymers could not function as displacer for these proteins. However, in the experiment these substances did work and the authors proposed a modified Langmuir model which introduces a hindrance factor , 6, which is negligible for the (small) displacer but significant for the proteins. As a result the isotherm system can be adjusted to appear normal . However, the exact physicochemical basis of this hindrance factor remains hidden. [Pg.71]


See other pages where Protein Trypsin is mentioned: [Pg.414]    [Pg.271]    [Pg.155]    [Pg.64]    [Pg.244]    [Pg.290]    [Pg.187]    [Pg.172]    [Pg.271]    [Pg.12]    [Pg.245]    [Pg.86]    [Pg.833]    [Pg.958]    [Pg.213]    [Pg.176]    [Pg.123]    [Pg.3420]    [Pg.106]    [Pg.756]    [Pg.73]    [Pg.110]    [Pg.31]   
See also in sourсe #XX -- [ Pg.240 ]




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Native protein structures bovine pancreatic trypsin inhibitor

Protein Engineering of Trypsin-Like Proteases

Protein Fragmentation Trypsin

Trypsin

Trypsin inhibitor protein

Trypsin protein digestion

Trypsin protein hydrolysis

Trypsin protein-derivatives hydrolysis

Trypsin trypsinization

Trypsin, protein digestion using

Trypsination

Trypsinization

Trypsinized proteins

Trypsinized proteins

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