Results 1 to 10 of about 3,419,991 (153)

Naturally Occurring Trypsin Inhibitors

1954
Publisher Summary This chapter discusses the following naturally occurring trypsin inhibitors: (1) pancreatic inhibitor of Kunitz and Northrop, (2) a second inhibitor from pancreas crystallized by Kazal, Spicer, and Brahinsky, (3) soybean inhibitor, (4) colostrum inhibitor, (5) lima bean inhibitor, (6) ovomucoid, (7) blood plasma inhibitor, and (8 ...
M, LASKOWSKI, M, LASKOWSKI
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Coevolution of insect trypsins and inhibitors

Archives of Insect Biochemistry and Physiology, 2004
AbstractMany plant proteinase inhibitors have lysine at the P1 position, presumably to avoid hydrolysis by insect trypsins. Lepidopteran trypsins appear to have adapted to resist proteinase inhibitors through increased inhibitor hydrolysis and decreased binding to inhibitor hydrophilic reactive sites.
A R, Lopes, M A, Juliano, L, Juliano, W R, Terra   +3 more
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Energy embedding of trypsin inhibitor

Biopolymers, 1982
AbstractEnergy 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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Trypsinogen, Trypsin, Trypsin-Substrate and Trypsin-Inhibitor Complexes in Urea Solutions

European Journal of Biochemistry, 1968
The denaturation in urea of trypsinogen, trypsin and trypsin derivatives is first-order with respect to protein. 1 Structural modifications affecting the trypsinogen molecule were detected by studying the influence of pH on the rate of denaturation. The acidification of trypsinogen leads to the appearance of 2 reversible equilibria I′⇌ II′⇌ III′
M, Delaage, M, Lazdunski
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Heat of reaction between trypsin and soybean trypsin inhibitor

Archives of Biochemistry and Biophysics, 1952
Abstract Calorimetric determinations of the heat of reaction between trypsin and soybean trypsin inhibitor protein indicate that ΔH for the reaction at 25 ° is 0 ± 1 kilocal./mole of trypsin reacted, if similar experiments with the inhibitor protein and bovine serum albumin are accepted as valid controls.
A, DOBRY, J M, STURTEVANT
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Interaction of Urinary Trypsin Inhibitor, UTI68, with Bovine Trypsin

The Journal of Biochemistry, 1982
One 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 ...
M, Tominaga, H, Takeda, M, Muramatu
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Trypsin, trypsinogen and trypsin inhibitor in human pancreatic juice

The American Journal of Medicine, 1960
Abstract 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, B, DYCE, H, BUNDY, H A, EDMONDSON   +3 more
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Interrelation of the urinary trypsin inhibitor to human plasma inter-alpha-trypsin inhibitor

Clinical Biochemistry, 1973
1. 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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On the Potential Role of Trypsin and Trypsin Inhibitors in Acute Pancreatitis

1984
The 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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Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor .beta.-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, and trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor

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,
P, Brandt, C, Woodward
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