Results 251 to 260 of about 341,861 (262)
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Biochemistry, 1987
Hydrogen exchange rates of six beta-sheet peptide amide protons in bovine pancreatic trypsin inhibitor (BPTI) have been measured in free BPTI and in the complexes trypsinogen-BPTI, trypsinogen-Ile-Val-BPTI, bovine trypsin-BPTI, and porcine trypsin-BPTI. Exchange rates in the complexes are slower for Ile-18, Arg-20, Gln-31, Phe-33, Tyr-35, and Phe-45 NH,
Clare Woodward, Pamela Brandt
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Hydrogen exchange rates of six beta-sheet peptide amide protons in bovine pancreatic trypsin inhibitor (BPTI) have been measured in free BPTI and in the complexes trypsinogen-BPTI, trypsinogen-Ile-Val-BPTI, bovine trypsin-BPTI, and porcine trypsin-BPTI. Exchange rates in the complexes are slower for Ile-18, Arg-20, Gln-31, Phe-33, Tyr-35, and Phe-45 NH,
Clare Woodward, Pamela Brandt
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Nature, 1964
Urinary Trypsin Inhibitor (Mingin): Transformation into a New Trypsin Inhibitor by Acid Hydrolysis or by ...
Uwe Nissen, Tage Astrup
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Urinary Trypsin Inhibitor (Mingin): Transformation into a New Trypsin Inhibitor by Acid Hydrolysis or by ...
Uwe Nissen, Tage Astrup
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Sunflower trypsin inhibitor‐1, proteolytic studies on a trypsin inhibitor peptide and its analogs
Peptide Science, 2010AbstractSunflower trypsin inhibitor‐1 (SFTI‐1) is a 14 amino acid cyclic peptide from sunflower seeds, which possesses exceptionally potent trypsin‐inhibitory activity, and has promise as a stable peptide‐based drug template. Within its compact structure, SFTI‐1 combines a head‐to‐tail cyclized backbone and a disulfide bond.
Richard J. Clark +5 more
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Interactions between trypsin, α2 macroglobulin and soybean trypsin inhibitor
Biochemical and Biophysical Research Communications, 1973Abstract The present study reveals that a trypsin- α 2 macroglobulin complex cannot be dissociated by the intervention of soybean trypsin inhibitor even after a 60 hour-incubation time. If the inhibitor is first bound to trypsin, the addition of α 2 macroglobulin restores about 60% of the enzyme activity.
Yvette Jacquot-Armand, Gisèle Krebs
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Inhibition by Trypsin Inhibitors of Dissociation of Embryonic Tissue by Trypsin
Nature, 1963TRYPSIN is used extensively for dissociation of tissues and in the preparation of suspensions of living cells1. The cell-dissociating effect of this enzyme has been attributed to tryptic degradation of cell binding materials1; however, theoretically, other possibilities exist and the question whether the characteristic enzymatic properties of trypsin ...
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2007
The sections in this article are 1 Introduction 2 Growing up with BPTI 3 Survey of Key NMR Experiments with BPTI 4 BPTI and NMR Spectroscopy with Proteins 5 BPTI and Resonance Assignments in Proteins 6 BPTI and Protein Structure Determination by NMR 7 BPTI and Amide Proton Exchange 8 BPTI and Internal Mobility in ...
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The sections in this article are 1 Introduction 2 Growing up with BPTI 3 Survey of Key NMR Experiments with BPTI 4 BPTI and NMR Spectroscopy with Proteins 5 BPTI and Resonance Assignments in Proteins 6 BPTI and Protein Structure Determination by NMR 7 BPTI and Amide Proton Exchange 8 BPTI and Internal Mobility in ...
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The effect of urea on the inhibition of trypsin by soybean trypsin inhibitor
Biochimica et Biophysica Acta, 1955Abstract The soybean inhibitor trypsin complex dissociates at pH 7.6 in the presence of urea. In experiments using a casein substrate containing urea in the same concentration as in Anson's hemoglobin method the dissociation constant was found to be about 2.2 10−9 M.
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Spectrophotometric Determination of Trypsin and Trypsin Inhibitors
Analytical Chemistry, 1957R. M. Hill, M. B. Rhodes, R. E. Feeney
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