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Self-hydrolysis

Second rare-earth series, 75 Self-assembled monolayer (SAM), 110 Self-hydrolysis process, 419 Self-propagating high temperature synthesis, 391... [Pg.525]

Autoiysis. Self-hydrolysis by tissue-degrading enzymes self-digestion. [Pg.644]

Homopolymers and both ethylacrylate and vinylacetate copolymers of 8-hydroxyqulnolyl acrylate, (5), gave large zones of inhibition in agar dish tests due to rapid self-hydrolysis from the polymers. Thus, the polymer systems are not suitable for slow release. Tests are underway on polymers of the extended chain analog, (6). [Pg.45]

Figure 7. Liposome-assisted catalysis. (A) Dependency of the initial hydrolysis rate of C16-O Np (nitrophenyl-pamitate) catalyzed by 1 mM carbobenzoxy-Phe-His-Leu-OH on the substrate concentration, in 0.05 M borate buffer pH 8.5. The filled circles are relative to the self-hydrolysis (no peptide, no liposomes). Open triangles are without liposomes, open squares with liposomes. (B) The pseudo-enzymatic turnover of the catalytically active liposomes. The catalytic activity results primarily from the binding (and solubilization) of a very hydrophobic histidin-containing peptide and the very hydrophobic substrate. Figure 7. Liposome-assisted catalysis. (A) Dependency of the initial hydrolysis rate of C16-O Np (nitrophenyl-pamitate) catalyzed by 1 mM carbobenzoxy-Phe-His-Leu-OH on the substrate concentration, in 0.05 M borate buffer pH 8.5. The filled circles are relative to the self-hydrolysis (no peptide, no liposomes). Open triangles are without liposomes, open squares with liposomes. (B) The pseudo-enzymatic turnover of the catalytically active liposomes. The catalytic activity results primarily from the binding (and solubilization) of a very hydrophobic histidin-containing peptide and the very hydrophobic substrate.
Thrombin of a high specific activity loses activity rapidly in a buffer solution without albumin, but remains active in an albumin solution (18). For example, the time dependence of thrombin activity in solutions is plotted in Figure 2, where activity changes of thrombin are compared in the absence of albumin and in the presence of 1 mg/ml albumin. In the absence of albumin, the effects of adsorption to a glass container as well as self-hydrolysis of thrombin seem to be detected within the initial 30 min, and then the effects of self-hydrolysis prevail. Therefore the data on the relative activities of thrombin in Table V are corrected on the basis of the data obtained from Figure 2. [Pg.84]

Chymotrypsin specifically cleaves peptide bonds whose C-terminal amino acid is adjacent to non-polar aromatic amino acid residues or the bulky, hydrophobic methionine. Because these residues are often buried in the interior of proteins, including chymotrypsin, the self-hydrolysis of native, folded chymotrypsin is very inefficient. In fact, during digestion, chymotrypsin acts most effectively on partially degraded and denatured (unfolded) proteins. [Pg.153]

NMR supports purity of the gel with correct integration ratio. The gel changed to powder on self-hydrolysis at room temperature. On pyrolysis at 350°C 50°C for 1 h in the presence of argon atmosphere it gives monodispersible powder with good crystallinity. [Pg.376]

First, cobalt particles are obtained with 2 moles of hydrogen after the reaction of cobalt salt and NaBH. Then, molybdenum particles precipitate and 6 moles of hydrogen gas are released. Later boron particles are precipitated and 5 moles of hydrogen gas are produced per 2 moles of NaBH. Finally the self hydrolysis reaction of NaBH occurs. [Pg.152]

Although less important, many other processes can be used—in particular, the flash self-hydrolysis that results from the explosion of shavings of wood impregnated with steam under pressure. [Pg.506]

A note on sensitivity should also be given in practical terms. Both resonances in an aqueous solution of aluminum sulfate can be observed at an aluminum concentration of M/800 after 24 000 scans. Both lines are broadened owing to self hydrolysis and the weaker one corresponds to a concentration of 0.0001 M. The spectrometer used in this case was a Bruker HX 400 operating at 104.2 MHz. [Pg.261]


See other pages where Self-hydrolysis is mentioned: [Pg.316]    [Pg.234]    [Pg.419]    [Pg.223]    [Pg.86]    [Pg.532]    [Pg.152]    [Pg.376]    [Pg.153]    [Pg.320]    [Pg.179]    [Pg.182]    [Pg.122]    [Pg.417]    [Pg.263]    [Pg.224]   
See also in sourсe #XX -- [ Pg.45 ]




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