scholarly journals The level and origin of amylase (EC 3.2.1.1) in the digestive tract of chicks receiving trypsin inhibitors in their diet

1978 ◽  
Vol 40 (2) ◽  
pp. 235-242 ◽  
Author(s):  
Zafrira Nitsan ◽  
Z. Madar
Keyword(s):  
Small Intestine ◽  
Digestive Tract ◽  
Intestinal Tract ◽  
Trypsin Inhibitors ◽  
Low Ph ◽  
Soya Bean ◽  
Amylase Secretion ◽  
Pancreatic Amylase ◽  
Bean Trypsin Inhibitor ◽  
Pancreatic Origin

1. Amylase (EC 3.2.1.1) activity found in the intestinal tract of chicks posterior to the stomach is of endogenous origin, as amylase in the food is inactivated by the low pH in the stomachs.2. Ingestion of raw soya-bean diet (RSD) or of heated soya-bean diet (HSD) supplemented with trypsin inhibitors induced higher amylase activities in the lower part of the small intestine and caecum as compared with HSD.3. Ingestion of RSD after ligation at the end of the duodenum, end of the ileum or one of the caeca, or injection of soya-bean trypsin inhibitor into a ligated caecum, indicated that there is no amylase synthesis by the intestinal tract cells or microflora as a response to the presence of RSD or trypsin inhibitors.4. It seems that amylase found in the digestive tract of the chick is of pancreatic origin and that RSD or trypsin inhibitors induce higher pancreatic amylase secretion than HSD which (the additional amylase) accumulates mainly in the caeca.

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.

Luminal Epidermal Growth Factor is Trophic to the Small Intestine of Parenterally Fed Rats

1995 ◽  
Vol 89 (2) ◽  
pp. 117-120 ◽  
Author(s):  
Tania Marchbank ◽  
Robert A. Goodlad ◽  
Chung Y. Lee ◽  
Raymond J. Playford
Keyword(s):  
Small Intestine ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Parenteral Nutrition ◽  
Trypsin Inhibitor ◽  
Soya Bean ◽  
Trophic Effect ◽  
Bean Trypsin Inhibitor ◽  
Epidermal Growth ◽  
Intestinal Atrophy

1. Intestinal atrophy contributes to the clinical difficulties of patients on parenteral nutrition. Systemic administration of epidermal growth factor reverses this effect, but there is concern over the clinical safety of intravenous administration of growth factors. We therefore investigated whether administration of luminal epidermal growth factor could reverse the atrophy induced in a rat model of parenteral nutrition when epidermal growth factor was given alone or in combination with soya bean trypsin inhibitor to reduce proteolytic digestion of the epidermal growth factor. 2. Infusion of soya bean trypsin inhibitor alone decreased intraluminal tryptic activity by about 90% but did not result in increased proliferation. Intragastric infusion of epidermal growth factor (72 μg/day per rat) caused a 26% increase in proliferation (determined by 2-h metaphase arrest) in the duodenum (P < 0.01) when compared with animals receiving ‘control’ intragastric infusion. However, intragastric epidermal growth factor had no effect on more distal regions of the bowel, probably reflecting rapid proteolysis of the epidermal growth factor by luminal proteases. In contrast, a trophic effect of luminal epidermal growth factor was seen in the duodenum (28% increase, P < 0.01) and jejunum (24% increase, P < 0.05) of animals which had received epidermal growth factor with soya bean trypsin inhibitor. This was probably due to the soya bean trypsin inhibitor decreasing the rate of degradation of epidermal growth factor by intestinal proteases, allowing biologically active epidermal growth factor to reach more distal portions of the bowel. 3. We conclude that luminal administration of epidermal growth factor in combination with protease inhibitors could provide a novel approach to the treatment of intestinal atrophy induced by parenteral nutrition. This approach may also be useful for the treatment of ulceration of the small intestine in conditions such as necrotizing enterocolitis or Crohn's disease. Clinical studies are recommended.

EFFECTS OF FAUNATION, PROTEIN SOURCE AND SURGICAL MODIFICATION OF THE INTESTINAL TRACT UPON FLOWS OF CALCIUM, PHOSPHORUS AND MAGNESIUM IN THE DIGESTIVE TRACT OF SHEEP

1988 ◽  
Vol 68 (3) ◽  
pp. 853-863 ◽  
Author(s):  
R. J. BOILA ◽  
G. D. PHILLIPS
Keyword(s):  
Small Intestine ◽  
Digestive Tract ◽  
Intestinal Tract ◽  
Bypass Surgery ◽  
Protein Source ◽  
Minimal Effect ◽  
Corn Gluten Meal ◽  
Corn Gluten ◽  
Calcium Phosphorus ◽  
P Absorption

Effects of faunation and protein source, corn gluten meal (CGM) versus soybean meal (SBM) upon Ca, P and Mg in the digestive tract of sheep were evaluated. Twelve yearling rams with cannulae in the abomasum and terminal ileum, and with sections of the small intestine bypassed (no bypass, n = 4; proximal third, n = 4; a distal third, n = 4) were used. All sheep were verified afaunated (protozoa-free) from birth; all sheep were faunated for the last half of the experiment. Negative Ca balances were obtained: for afaunated (P < 0.01) relative to faunated sheep, with less (P < 0.01) Ca absorbed in the stomach section and more (P < 0.01) Ca secreted in the large intestine of afaunated sheep; and for SBM (P = 0.07) as opposed to CGM fed sheep, with less (P < 0.01) Ca absorbed in the stomach section of SBM sheep. With SBM fed, afaunated sheep, the Ca balance was the same as that measured in all proximal bypass sheep. Proximal bypass surgery had a minimal effect (0.10 > P > 0.05), while protein source had no (P > 0.05) influence upon P or Mg. Faunation influenced P secretion (P < 0.05) and Mg absorption (P < 0.05) in the stomach section, and P absorption (P < 0.05) in the small intestine. More dietary P (P < 0.05) and Mg (P < 0.01) was absorbed from the digestive tract of faunated than afaunated sheep. Key words: Sheep, faunation, calcium, phosphorus, magnesium, digestion

scholarly journals Digestion in the pig between 7 and 35 d of age

1981 ◽  
Vol 45 (2) ◽  
pp. 321-336 ◽  
Author(s):  
R. H. Wilson ◽  
Jane Leibholz
Keyword(s):  
Small Intestine ◽  
Milk Protein ◽  
Intestinal Tract ◽  
Live Weight ◽  
Mean Value ◽  
Soya Bean ◽  
Protein Source ◽  
Liquid Form ◽  
Gastro Intestinal Tract ◽  
Bean Protein

1. In two separate experiments, forty-four pigs weaned at 4–5 d of age were given diets containing milk or soya-bean proteins until slaughtered at 14, 28 or 35 d of age.2. The retention times of digesta in the stomach and the entire gastro-intestinal tract did not differ between pigs given pelleted diets containing milk or soya-bean protein.3. Digesta retention times in the stomach were shorter (61 v. 146 min) in pigs given a milk-protein diet in a liquid form than in pigs given the same diet in a pelleted form. The retention times in the whole gastro-intestinal tract were 42.8 v. 29.6 h on the respective diets.4. The total retention time of digesta in the gastro-intestinal tract increased with age of pigs between 14–35 d of age when given pelleted diets but not when given a liquid diet.5. The daily amount of digesta flowing through the anterior small intestine was unaffected by the source of protein. Greater endogenous secretions into the anterior small intestine were observed when pigs were fed ad lib. than when fed at 2 g nitrogen (45 g dry matter (DM))/kg live weight0.75 per d.6. The apparent digestion of DM to the ileum of pigs given milk, isolated soya-bean protein (ISP) (Promine D) or soya-bean meal (SBM) protein at 28 d of age was 0.826, 0.825 and 0.644 respectively.7. The apparent digestion of DM to the ileum of pigs given ISP (Supro 610) significantly increased with age of pigs from 0.851 at 14 d of age to 0.883 at 35 d of age. No increase was observed for pigs given milk protein.8. Differences in the digestibility of DM between protein sources were greater to the ileum than over the entire gastro-intestinal tract. The greatest increase in DM digestion from the ileum to the faeces occurred in pigs given SBM (0.644–0.874).9. Neither the protein source nor age of pigs influenced gastric pH values, the mean value being 4.05. pH increased along the small intestine and was not affected by the protein source or age of pig.

Cold Promoted Activation of Factor VII VI. Effect of Inhibitors

1973 ◽  
Vol 29 (03) ◽  
pp. 633-643
Author(s):  
H Gjønnæss
Keyword(s):  
Soya Bean ◽  
Factor Vii ◽  
Plasma Kallikrein ◽  
Contact Activation ◽  
Activation Reaction ◽  
Hexadimethrine Bromide ◽  
Bean Trypsin Inhibitor ◽  
Plasma Arginine ◽  
Kallikrein Activity ◽  
Effect Of Inhibitors

SummaryThe cold promoted activation of factor VII occurs in parallel with an activation of a plasma arginine esterase, and, on inhibition of the cold activation of factor VII, the esterase activation also decreased. The inhibitor pattern supported our theory that the arginine esterase that is activated in the cold activation of factor VII is plasma kallikrein.The cold activation of factor VII was completely inhibited with soya bean trypsin inhibitor in doses that did not interfere with the contact activation. On the other hand, inhibition of the contact activation with hexadimethrine bromide did not interfere with the cold activation of factor VII except when this was kaolin induced. Contact and cold activation therefore appear to represent two different pathways for the activation of factor VII. The cold activation reaction is probably mediated by the activation of plasma prekallikrein, and inhibition of the plasma kallikrein activity correlates with the inhibition of the cold promoted activation of factor VII.

Anatomi Saluran Pencernaan biawak air (Varanus salvator) (Reptil: Varanidae)

2019 ◽  
Author(s):  
Mahfud Mahfud ◽  
Ihwan
Keyword(s):  
Small Intestine ◽  
Digestive Tract ◽  
Large Intestine ◽  
Scientific Information ◽  
Tissue Perfusion ◽  
Animal Population ◽  
Varanus Salvator ◽  
Commercial Purpose ◽  
Left And Right ◽  
Biology Laboratory

Excessive hunting and poaching for commercial purpose of Varanus salvator in Indonesia can cause a decline in this animal population. However, the scientific information of this animal especially about the biologic of organ system is rarely reported. Therefore, this case opens up opportunities for researching, which aims to study the anatomy of digestive tract of water monitor macroscopically. This research has been conducted in Biology Laboratory, University of Muhammadiyah Kupang for 5 months from March to August 2016. The digestive organ of this animal that has been preserved in alcohol 70% was obtained before from two males of water monitors. Preservation process: the animal were anesthetized, exsanguinated, and fixated in 4 paraformaldehyde by tissue perfusion method. Observations were performed to the visceral site and morphometrical of digestive tract. The resulted data was analysed descriptively and presented in tables and figures. The digestive tract of water monitor consist of esophagus, stomach, small intestine, large intestine and cloaca. The dimension of each organ is different based on its structures and functions. The esophagus of water monitor connects the mouth cavity and the stomach and also as the entrance of food to the stomach. Water monitor stomach were found in cranial part of abdomen, in left side of liver. The small intestine was longer than stomach and it is a winding muscular tube in abdomen in posterior side of liver. The large intestine consist of colon and cloaca, while cecum was not found. This channel was extend lateromedially in abdomen to cloaca between left and right kidneys. The cloaca was the end of digestive tract which excreted feces and urine. From this research, we can conclude that the digestive tract of water monitor consists of esophagus, stomach, small intestine, and large intestine. It’s difficult to differentiate small intestine and large intestine because there are no cecum.

Activation of latent collagenase from polymorphonuclear leukocytes by cathepsin G

1979 ◽  
Vol 44 (10) ◽  
pp. 3177-3182 ◽  
Author(s):  
Mária Stančíková ◽  
Karel Trnavský
Keyword(s):  
Affinity Chromatography ◽  
Trypsin Inhibitor ◽  
Polymorphonuclear Leukocytes ◽  
Soya Bean ◽  
Cathepsin G ◽  
Sepharose Column ◽  
Bean Trypsin Inhibitor ◽  
Human Polymorphonuclear Leukocytes

Cathepsin G was isolated from human polymorphonuclear leukocytes and purified by affinity chromatography on Antilysin-Sepharose column. Purified enzyme activated later collagenase isolated from leukocytes. Activation at 36°C was maximal after 30 min incubation. Inhibitors of cathepsin G - soya-bean trypsin inhibitor, diisopropyl phosphofluoridate and Antilysin were active in inhibiting the activation of latent collagenase by cathepsin G.

scholarly journals The digestion by cattle of silage-containing diets fed at two dry matter intakes

1985 ◽  
Vol 54 (2) ◽  
pp. 483-492 ◽  
Author(s):  
H. A. Greife ◽  
J. A. Rooke ◽  
D. G. Armstrong
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Dry Matter ◽  
Soya Bean ◽  
Rumen Bacteria ◽  
Bean Meal ◽  
Soya Bean Meal

1. In a 4 x 4 Latin square experiment four cows were given, twice daily, diets consisting of (g/kg dry matter (DM)) 500 barley, 400 grass silage and 100 soya-bean meal. The diets were given at either 1.15 (L) or 2.3 (H) times maintenance energy requirements and the soya-bean meal was either untreated (U) or formaldehyde (HCH0)-treated (T).2. The passage of digesta to the duodenum was estimated using chromic oxide as a flow marker;35S was used to estimate the amount of microbial protein entering the small intestine. A microbial fraction was prepared by differential centrifugation from duodenal digesta. Samples of bacteria and of protozoa from rumen digesta were also prepared.3. The total amino acid contents of feedingstuffs, duodenal digesta, duodenal microbial material, rumen bacteria and rumen protozoa were determined by ion-exchange chromatography. The D-alanine and D-glutamic acid contents of the samples were determined by gas–liquid chromatography.4. The quantity of each amino acid entering the small intestine was significantly (P < 0,001) increased by increasing DM intake and tended to be increased by formaldehyde-treatment of the soya-bean meal. There were net losses of all amino acids across the forestomachs except for lysine, methione, o-alanine and D-glutamic acid for which there were net gains.5. There were significant (P < 0.05) differences in amino acid composition between rumen bacteria and duodenal microbial material; differences in amino acid composition between rumen bacteria and rumen protozoa were also observed.6. D-Alanine and D-glutamic acid were present in the silage but not in the barley or either of the soya-bean meals. All samples of microbes and digesta contained D-alanine and D-glutamic acid.7. The use of D-ahine and D-glUtamiC acid as markers for microbial nitrogen entering the small intestine was assessed. Estimates of the quantities of microbial N entering the small intestine based on the D-alanine or D-glutamic acid contents of rumen bacteria or duodenal microbes were significantly higher than those determined using 35S as a marker.

scholarly journals Acute Low-Intensity Treadmill Running Upregulates the Expression of Intestinal Glucose Transporters via GLP-2 in Mice

Nutrients ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 1735
Author(s):  
Kai Aoki ◽  
Takuji Suzuki ◽  
Fang Hui ◽  
Takuro Nakano ◽  
Koki Yanazawa ◽  
...  
Keyword(s):  
Small Intestine ◽  
Intestinal Tract ◽  
Glucose Transporter ◽  
Treadmill Running ◽  
Low Intensity ◽  
Glucose Transporter 2 ◽  
Intestinal Digestion ◽  
Glucagon Like Peptide ◽  
Low Intensity Exercise ◽  
Carbohydrate Digestion

The effects of exercise on nutrient digestion and absorption in the intestinal tract are not well understood. A few studies have reported that exercise training increases the expression of molecules involved in carbohydrate digestion and absorption. Exercise was also shown to increase the blood concentration of glucagon-like peptide-2 (GLP-2), which regulates carbohydrate digestion and absorption in the small intestine. Therefore, we investigated the effects of exercise on the expression of molecules involved in intestinal digestion and absorption, including GLP-2. Six-week-old male mice were divided into a sedentary (SED) and low-intensity exercise (LEx) group. LEx mice were required to run on a treadmill (12.5 m/min, 1 h), whereas SED mice rested. All mice were euthanized 1 h after exercise or rest, and plasma, jejunum, ileum, and colon samples were collected, followed by analysis via IHC, EIA, and immunoblotting. The levels of plasma GLP-2 and the jejunum expression of the GLP-2 receptor, sucrase-isomaltase (SI), and glucose transporter 2 (GLUT2) were higher in LEx mice. Thus, we showed that acute low-intensity exercise affects the expression of molecules involved in intestinal carbohydrate digestion and absorption via GLP-2. Our results suggest that exercise might be beneficial for small intestine function in individuals with intestinal frailty.

Sign in / Sign up

Export Citation Format

Share Document