Results 331 to 340 of about 256,479 (340)

Sunflower trypsin inhibitor‐1, proteolytic studies on a trypsin inhibitor peptide and its analogs

Peptide Science, 2010
AbstractSunflower 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, Michael L. J. Korsinczky, Fiona Foley, David J. Craik, Michelle L. Colgrave, Michelle L. Colgrave   +5 more
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Interactions between trypsin, α2 macroglobulin and soybean trypsin inhibitor

Biochemical and Biophysical Research Communications, 1973
Abstract 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, 1963
TRYPSIN 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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Alfalfa trypsin inhibitor

Journal of Agricultural and Food Chemistry, 1978
Gerald R. Reeck, H.L. Mitchell, Hsin-Yi Chang   +2 more
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Pancreatic Trypsin Inhibitor

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 effect of urea on the inhibition of trypsin by soybean trypsin inhibitor

Biochimica et Biophysica Acta, 1955
Abstract 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, 1957
R. M. Hill, M. B. Rhodes, R. E. Feeney
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TRYPSIN INHIBITORS

The Lancet, 1970
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THE MECHANISM OF FORMATION OF A TRYPSIN‐TRYPSIN INHIBITOR COMPLEX^*

Annals of the New York Academy of Sciences, 1968
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Studies on Crystalline Trypsin, Soybean Trypsin Inhibitor and Inhibitor-Trypsin Compound with the Ultracentrifuge^1,2

Journal of the American Chemical Society, 1953
A. D. McLaren, Erwin Sheppard
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