scholarly journals Discrepancy between the potency of various trypsin inhibitors to inhibit trypsin activity and the potency to release biologically active cholecystokinin-pancreozymin.

1984 ◽  
Vol 34 (5) ◽  
pp. 849-856 ◽  
Author(s):  
Hidetoshi YONEZAWA
Keyword(s):  
Trypsin Inhibitors ◽  
Biologically Active ◽  
Trypsin Activity ◽  
Inhibit Trypsin Activity

scholarly journals Trypsin inhibitors in turnip (Brassica rapa L.) seeds

2014 ◽  
Vol 58 (4) ◽  
pp. 563-573 ◽  
Author(s):  
Anna Wilimowska-Pelc
Keyword(s):  
Molecular Weight ◽  
Peptide Bond ◽  
Ion Exchange Chromatography ◽  
Trypsin Inhibitors ◽  
Exchange Chromatography ◽  
Trypsin Activity ◽  
Reactive Site ◽  
Salting Out ◽  
Similar Molecular Weight ◽  
Immobilized Trypsin

A method of trypsin inhibitors isolation from turnip seeds is described. Inhibitors were extracted with 0.01 N HCI, concentrated by salting out with ammonium sulfate, and purified using ion-exchange chromatography on Sp-Sephadex C-25, QAE-Sephadex A-25 and affinity chromatography on immobilized trypsin. Among the three isolated inhibitors, ITR I of molecular weight 15.9 kDa, pl. 6,4, inhibited trypsin activity only. Inhibitors ITR II and ITR Ill inhibited also chymotrypsin activity, they had similar molecular weight (about 10 kDa), but their pI is 7.5 and over 10, respectively. Arginine residue occurred in P, position of the reactive site of inhibitors ITR I and ITR III, while in ITR 11 this position was occupied by lysine residue. Electrophoresis on polyacrylamide gel revealed that each inhibitor possessed two protein fractions, probably a virgin and modified form, with the reactive site peptide bond broken by trypsin.

TWO DERIVATIVES OF POLY(ACRYLIC ACID) ARE ABLE TWO INHIBIT TRYPSIN ACTIVITY

1994 ◽  
pp. 316
Author(s):  
H.L. Lueβen ◽  
J.C. Verhoef ◽  
C.-M. Lehr ◽  
A.G. de Boer ◽  
H.E. Junginger
Keyword(s):  
Acrylic Acid ◽  
Trypsin Activity ◽  
Derivatives Of ◽  
Inhibit Trypsin Activity ◽  
Poly Acrylic Acid

P8 Two derivatives of poly(acrylic acid) are able to inhibit trypsin activity

1994 ◽  
Vol 29 (3) ◽  
pp. 388-389
Author(s):  
H.L. Lueßen ◽  
J.C. Verhoef ◽  
C.-M. Lehr ◽  
A.G. de Boer ◽  
H.E. Junginger
Keyword(s):  
Acrylic Acid ◽  
Trypsin Activity ◽  
Derivatives Of ◽  
Inhibit Trypsin Activity ◽  
Poly Acrylic Acid

scholarly journals The effect of trypsin inhibitors on pancreatopeptidase E, trypsin, chymotrypsin and amylase in the pancreas and intestinal tract of chicks receiving raw and heated soya-bean diets

1970 ◽  
Vol 24 (4) ◽  
pp. 893-904 ◽  
Author(s):  
A. Gertler ◽  
Zafrira Nitsan
Keyword(s):  
Growth Rate ◽  
Small Intestine ◽  
Proteolytic Activity ◽  
Intestinal Tract ◽  
Proteolytic Enzymes ◽  
Trypsin Inhibitors ◽  
Soya Bean ◽  
Trypsin Activity ◽  
Pancreas Weight ◽  
Slight Depression

1. Feeding on a raw soya-bean diet (RSD) increased the levels of trypsin, chymotrypsin and pancreatopeptidase E but decreased the level of amylase in the pancreas of chicks as compared to a heated soya-bean diet (HSD), while supplementation of HSD with soya-bean trypsin inhibitors increased the activity of all four enzymes. HSD + trypsin inhibitors caused significant enlargement of the pancreas but only a slight depression in growth rate.2. Fasting for 24 h of chicks previously given RSD and HSD increased the activity of all four enzymes but the increase was much greater in chicks previously given RSD than in those previously given HSD.3. Feeding RSD for 4 d to chicks previously adapted to HSD resulted in a dramatic inhibition in growth rate, a small increase in pancreas weight, and an increase in the activity of all proteolytic enzymes, while no change in the amylase was detectable.4. Trypsin, chymotrypsin and pancreatopeptidase E activities were assayed in the contents of the small intestine and caecum of chicks fed on RSD or HSD over a period of 35 d. Trypsin and chymotrypsin activities in the small intestine were lower in chicks fed on RSD while pancreatopeptidase E activity was almost equal or even higher in RSD-fed chicks, especially at the age of 35 d. Trypsin activity in the caecum of RSD-fed chicks was lower at all stages of the experiment, while the pancreatopeptidase E and chymotrypsin activities in the caecum of RSD-fed chicks exceeded the levels in the HSD group at the age of 21 and 35 d respectively. It would appear therefore that pancreatopeptidase E may play an important part in overcoming the inhibition of the proteolytic activity in the intestine of chicks fed on RSD.

scholarly journals MODIFICATION OF THE GELATIN SUBSTRATE PROCEDURE FOR DEMONSTRATION OF ACROSOMAL PROTEOLYTIC ACTIVITY

1972 ◽  
Vol 20 (7) ◽  
pp. 499-506 ◽  
Author(s):  
ARTHUR PENN ◽  
BARTON L. GLEDHILL ◽  
ZBIGNIEW DARŻYNKIEWICZ
Keyword(s):  
Proteolytic Activity ◽  
Trichloroacetic Acid ◽  
Mammalian Species ◽  
Trypsin Activity ◽  
Diisopropyl Fluorophosphate ◽  
Sperm Sample ◽  
Biochemical Studies ◽  
Inhibit Trypsin Activity

In situ proteolytic activity in the heads of sperm of seven mammalian species has been demonstrated using autoradiographic film as a gelatin substrate. The film is first exposed and processed and then coated with the sperm sample. Proteolytic activity is monitored by following the appearance of "halos," which are areas of gelatin digestion and are found to surround the heads of reacting sperm. The proteolytic factor appears to be released from the acrosome and may be the protease with trypsin-like activity that has been found associated with the acrosome in biochemical studies. l-Chloro-3-tosylamido-7-amino-2-heptanone and diisopropyl fluorophosphate, both of which inhibit trypsin activity, apparently interact with a substance released from the acrosome but do not interfere with the formation of halos. Sperm treated with trichloroacetic acid, urea or formalin do not form halos.

scholarly journals Screening of antinutrients in leaves, fruit pulp and seeds of Gishta (Annona spp.) of Ethiopia, North East Africa

2016 ◽  
Vol 4 (3) ◽  
pp. 471
Author(s):  
Harikrishna Ramaprasad Saripalli ◽  
Prasanna Kumar Dixit
Keyword(s):  
Human Consumption ◽  
Cyanogenic Glycosides ◽  
Chemical Analyses ◽  
Fruit Pulp ◽  
Trypsin Activity ◽  
Plant Materials ◽  
North East ◽  
High Concentrations ◽  
Inhibit Trypsin Activity ◽  
Seed Extracts

<div><p><em>Graviola or Gishta (Annona spp. of Ethiopia) are generally useful for human consumption were analysed for the presence of potentially harmful chemicals (antinutrients) and for their toxicity. The purpose of the study was to determine whether the Graviola or Gishta (Annona spp. of Ethiopia) leaves, fruit pulp and seed extracts were safe for human consumption. Chemical analysis showed that none of  tested parts contained cyanogenic glycosides, however all the three tested plant materials contained oxalic acid in high concentrations and also  contained negligible amounts of phytic acid, saponins and alkaloids. Tested plant samples also found to inhibit trypsin activity. These chemical analyses were carried out in duplicate.</em></p></div>

Two derivatives of poly(acrylic acid) are able two inhibit trypsin activity

1994 ◽  
Vol 28 (1-3) ◽  
pp. 316
Author(s):  
H.L. Lueßen ◽  
J.C. Verhoef ◽  
C.-M. Lehr ◽  
A.G. de Boer ◽  
H.E. Junginger
Keyword(s):  
Acrylic Acid ◽  
Trypsin Activity ◽  
Derivatives Of ◽  
Inhibit Trypsin Activity ◽  
Poly Acrylic Acid

Proteins but not amino acids, carbohydrates, or fats stimulate cholecystokinin secretion in the rat

1986 ◽  
Vol 251 (2) ◽  
pp. G243-G248 ◽  
Author(s):  
R. A. Liddle ◽  
G. M. Green ◽  
C. K. Conrad ◽  
J. A. Williams
Keyword(s):  
Amino Acids ◽  
Bovine Serum Albumin ◽  
Trypsin Inhibitor ◽  
Simultaneous Administration ◽  
Trypsin Activity ◽  
Intact Proteins ◽  
Plasma Cholecystokinin ◽  
Inhibit Trypsin Activity ◽  
Cck Release

Because of prior difficulties in measuring plasma cholecystokinin (CCK) levels, it has not been established which components of food stimulate CCK secretion in rats. In the present study, we used a sensitive and specific bioassay for measuring plasma CCK and determined the effects of proteins, protein hydrolysates, amino acids, fats, starch, and glucose on CCK secretion in this species. Intact proteins were the only stimulants of CCK release. Solutions of 18% casein and 0.2% soybean trypsin inhibitor caused prompt increases in plasma CCK levels from 0.5 +/- 0.2 to 7.9 +/- 1.9 and 8.0 +/- 2.0 pM, respectively, within 5 min of orogastric administration. The proteins lactalbumin and bovine serum albumin caused smaller elevations in circulating CCK. In contrast, hydrolysates of casein and lactalbumin and the amino acids L-phenylalanine and L-tryptophan did not stimulate CCK release. In addition, plasma CCK levels did not increase with the feeding of fat, starch, or glucose. The ability of proteins to stimulate CCK secretion paralleled their ability to inhibit trypsin activity in vitro. Furthermore, the plasma CCK response to casein was completely abolished by the simultaneous administration of trypsin. These studies indicate that proteins are the major food stimulants of CCK release in the rat and that the effects of proteins are related to inhibition of intraluminal protease activity.

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