Results 391 to 400 of about 712,349 (416)
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TRYPSIN AND TRYPSIN INHIBITORS FROM PENAEID SHRIMP
Journal of Food Biochemistry, 2002Trypsin inhibitors from four species of shrimp, P. vannamei, P. monodon, P. stylirostris, and P. californiensis were characterized by test tube and electrophoretic assays. Inhibitors in the four phylogenetically related species showed different inhibitory capacity and specificity for orthologous trypsins. Inhibitors from P.
Cristiane De Albuquerque-Cavalcanti +2 more
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Novel trypsin-FITC@MOF bioreactor efficiently catalyzes protein digestion.
Journal of materials chemistry. B, 2013A simple nanoporous metal organic framework (MOF) bioreactor preparation via a low energy 30 minute vortex as driving force to immobilize trypsin enzyme is presented. No chemical modifications were employed thus organic wastes were eliminated.
Wan-Ling Liu +5 more
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Nanoscale, 2013
On the basis of cytochrome c-induced self-assembled graphene quantum dots, we demonstrate a novel fluorescent biosensor for trypsin with remarkable fluorescence enhancement, as well as high selectivity and sensitivity.
Xing Li +6 more
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On the basis of cytochrome c-induced self-assembled graphene quantum dots, we demonstrate a novel fluorescent biosensor for trypsin with remarkable fluorescence enhancement, as well as high selectivity and sensitivity.
Xing Li +6 more
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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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Interaction of Urinary Trypsin Inhibitor, UTI68, with Bovine Trypsin
The Journal of Biochemistry, 1982One molecule of UTI68, a trypsin inhibitor purified from urine of healthy men, inhibited four molecules of bovine trypsin. This finding suggests the formation of various complexes of UTI68 with 1 to 4 molecules of trypsin. However, SDS polyacrylamide gel electrophoresis of the reaction products of UTI68 with trypsin showed that, at molecular ratios of ...
Mutumi Muramatu +2 more
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Phase transfer surfactant-aided trypsin digestion for membrane proteome analysis.
Journal of Proteome Research, 2008We have developed a new protocol for digesting hydrophobic proteins using trypsin with the aid of phase-transfer surfactants (PTS), such as sodium deoxycholate (SDC). SDC increases the solubility of hydrophobic proteins, enhances the activity of trypsin,
Takeshi Masuda, M. Tomita, Y. Ishihama
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Nature Immunology, 2002
The α-defensins from Paneth cells in intestinal crypts need processing to be fully functional. Unlike for mice, the cleaving enzyme for human HD5 turns out to be trypsin.
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The α-defensins from Paneth cells in intestinal crypts need processing to be fully functional. Unlike for mice, the cleaving enzyme for human HD5 turns out to be trypsin.
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On the Potential Role of Trypsin and Trypsin Inhibitors in Acute Pancreatitis
1984The protective role of alpha 2-macroglobulin, alpha 1-antitrypsin and Aprotinin against trypsin-induced effects on C3 and kininogen was studied in a human in vitro model. When human cationic trypsin was added to human serum or plasma, there was a gradual saturation of alpha 2-macroglobulin and later of alpha 1-antitrypsin.
Åke Lasson, Kjell Ohlsson
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1973
Publisher Summary This chapter discusses the use of trypsin in cultures of mammalian tissues. Trypsin is a pancreatic proteolytic enzyme that preferentially catalyzes the hydrolysis of peptide bonds between the carboxy group of arginine or lysine and the amino group of another amino acid.
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Publisher Summary This chapter discusses the use of trypsin in cultures of mammalian tissues. Trypsin is a pancreatic proteolytic enzyme that preferentially catalyzes the hydrolysis of peptide bonds between the carboxy group of arginine or lysine and the amino group of another amino acid.
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The preparation and properties of two new chromogenic substrates of trypsin.
Archives of Biochemistry and Biophysics, 1961B. Erlanger +2 more
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