Results 281 to 290 of about 259,629 (307)
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Energy embedding of trypsin inhibitor
Biopolymers, 1982AbstractEnergy embedding has been shown recently to be a useful extension of the distance geometry approach to conformational calculations in the case of very small molecules and simple energy functions. This paper tests the ability of energy embedding to locate low energy conformations satisfying both weak and strong geometric constraints when the ...
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Trypsin, trypsinogen and trypsin inhibitor in human pancreatic juice
The American Journal of Medicine, 1960Abstract 1.1. Benzoylarginine-paranitroanilide was employed as substrate in a method which permits simple, sensitive and rapid assay of trypsin. 2.2. Human pancreatic juice obtained by catheter drainage of the duct of Wirsung exhibited no spontaneous tryptic activity.
B J, HAVERBACK +3 more
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Interrelation of the urinary trypsin inhibitor to human plasma inter-alpha-trypsin inhibitor
Clinical Biochemistry, 19731. Immunological investigations were conducted with specific antisera to the urinary trypsin inhibitor (UTI) and human plasma trypsin inhibitors. The results indicated that UTI is not interrelated to either α 1 -anti-trypsin or α 2 -macroglobulin, the main plasma trypsin inhibitors. UTI appears to be interrelated with inter- α -trypsin inhibitor (
G J, Proksch, J, Lane, C D, Nordschow
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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.
Colgrave, Michelle +4 more
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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.
A, Lasson, K, Ohlsson
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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.
G, Krebs, Y, Jacquot-Armand
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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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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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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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