• Title/Summary/Keyword: Digestive Enzyme

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Effect of Heavy Metals on the Secretion of Amylase in Rat Pancreatic Fragments (중금속류가 취절편의 Amylase 분비에 미치는 영향)

  • Kim, Hea-Young;Kim, Won-Joon
    • The Korean Journal of Pharmacology
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    • v.17 no.2
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    • pp.31-36
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    • 1981
  • Heavy metals which are present as trace elements in human body have been known to modify various enzymatic reaction. These metals can be essential or non-essential. Zinc, copper and calcium are essential in maintaining some biological processes, whereas non-essential metals such as cadmium, lead and mercury produce accumulatve toxic effect. Cadmium accumulated in pancreas can cause toxicity and damage of pancreatic cells, thereby influencing CHO metabolism. Lead compounds are known to produce toxic effects on the kidney, digestive system and brain fellowed by inhibition of activity of ${\rho}-aminolevulinic$ acid and biosynthesis of hemoproteins and cytochrome. Evidence has been accumulated that zinc not only acts as a cofactor in enzyme reaction but also prevents toxic effect induced by heavy metal such as copper and cadmium. To demonstrate the effect of heavy metals on pancreatic secretion, part of uncinate pancreas was taken and incubated in Krebs-Ringer bicarbonate buffer with heavy metals used. Additional treatment with CCK-OP was performed when needed. After incubation during different period of time, medium was analyzed for amylase activity using Bernfeld's method. The present study was attempted in order to elucidate the effect of several kinds of heavy metal on exocrine pancreatic secretion in vitro. The results obtained are as follows: 1) CCK-OP stimulated significantly amylase release from pancreatic fragments in vitro. 2) CCK-OP response of amylase release from pancreatic fragments was inhibited by treatmant with cadmium, especially high doses of cadmium. 3) CCK-OP response of amylase release from pancreatic fragments was inhibited when pretreated with $10^{-4}M$ copper chloride. 4) Lead chloride at the concentration of $10^{-3}M\;and\;10^{4}M$ stimulated the basal amylase release in vitro but CCK-OP response did not augment by lead chloride. 5) Zine chloride did not affect amylase release from pancreatic fragment in vitro. From the results mentioned above, it is suggested that CCK-OP response was inhibited it the amylase release from pancreatic fragments pretreated with cadmium and copper chloride.

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A NOTE ON THE REMOVAL OF PHYTATE IN SOYBEAN MEAL USING Aspergillus usami

  • Ilyas, A.;Hirabayasi, M.;Matsui, T.;Yano, H.;Yano, F.;Kikishima, T.;Takebe, M.;Hayakawa, K.
    • Asian-Australasian Journal of Animal Sciences
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    • v.8 no.2
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    • pp.135-138
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    • 1995
  • Soybean meal was fermented by Aspergillus usami in order to reduce phytate content. Aflatoxin B1 was not detected in the fermented soybean meal. The contents of crude protein, crude fiber, ether extract and crude ash were slightly increased following fermentation with a concomitant reduction in nitrogen free extract. Though the fermentation partly degraded proteins in the soybean meal, there was small difference in amino acid composition between the soybean meal and the fermented soybean meal. The results showed that the fermentation did not affect nutritional value of protein in soybean meal. Approximately 55% of phosphorus extracted by trichloroacetic acid was inositol hexaphosphate (phytate) in the soybean meal. The content of inositol tetra to hexaphosphates was not detected in the fermented soybean meal. These results indicated that the fermentation almost completely eliminated phytate in soybean meal. Phytase activity was not detected in the unfermented soybean meal. However, the enzyme activity in the fermented soybean meal was 167.7 U/g. When the fermented soybean meal in supplemented in formula feeds, phytase in the fermented soybean meal might partly degrade the phytate in other ingredients in the digestive tract. The fermented soybean meal is possibly used as a phytate-free protein source of feed, which contains high available phosphorus.

Inhibition of Trypsin-Induced Mast Cell Activation by Water Fraction of Lonicera japonica

  • Kang, Ok-Hwa;Choi, Yeon-A;Park, Hye-Jung;Lee, Joo-Young;Kim, Dae-Ki;Choi, Suck-Chei;Kim, Tae-Hyun;Nah, Yong-Ho;Yun, Ki-Jung;Choi, Suck-Jun;Kim, Young-Ho;Bae, Ki-Hwan;Lee, Young-Ml
    • Archives of Pharmacal Research
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    • v.27 no.11
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    • pp.1141-1146
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    • 2004
  • Lonicera japonica Thunb.(Caprifoliaceae) has long been known as an anti-inflammatory. In the present study, the effect of water fraction of Lonicera japonica (LJ) on trypsin-induced mast cell activation was examined. HMC-1 cells were stimulated with trypsin (100 nM) in the presence or absence of LJ (10, 100, and 1000 $\mu$ g/mL). TNF-$\alpha$ and tryptase production were measured by enzyme-linked immunosorbent assay (ELISA) and reverse transcription-PCR. Extracellular signal-regulated kinase (ERK) phosphorylation was assessed by Western blot. Trypsin activity was measured by using Bz-DL-Arg-p-nitroanilide (BAPNA) as substrate. LJ (10, 100, and 1000 $\mu$g/mL) inhibited TNF-$\alpha$ secretion in a dose-dependent manner. LJ (10, 100, and 1000 $\mu$g/mL) also inhibited TNF-$\alpha$ and tryptase mRNA expression in trypsin-stimulated HMC-1. Furthermore, LJ inhibited trypsin-induced ERK phosphorylation. However, LJ did not affect the trypsin activity even 1000 $\mu$g/mL. These results indicate that LJ may inhibit trypsin-induced mast cell activation through the inhibition of ERK phosphorylation than the inhibition of trypsin activity.

Evaluation of the MTHFR C677T Polymorphism as a Risk Factor for Colorectal Cancer in Asian Populations

  • Rai, Vandana
    • Asian Pacific Journal of Cancer Prevention
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    • v.16 no.18
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    • pp.8093-8100
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    • 2016
  • Background: Genetic and environmental factors play important roles in pathogenesis of digestive tract cancers like those in the esophagus, stomach and colorectum. Folate deficiency and methylenetetrahydrofolate reductase (MTHFR) as an important enzyme of folate and methionine metabolism are considered crucial for DNA synthesis and methylation. MTHFR variants may cause genomic hypomethylation, which may lead to the development of cancer, and MTHFR gene polymorphisms (especially C677T and A1298C) are known to influence predispositions for cancer development. Several case control association studies of MTHFR C677T polymorphisms and colorectal cancer (CRC) have been reported in different populations with contrasting results, possibly reflecting inadequate statistical power. Aim: The present meta-analysis was conducted to investigate the association between the C677T polymorphism and the risk of colorectal cancer. Materials and Methods: A literature search of the PubMed, Google Scholar, Springer link and Elsevier databases was carried out for potential relevant articles. Pooled odds ratio (OR) with corresponding 95 % confidence interval (95 % CI) was calculated to assess the association of MTHFR C677T with the susceptibility to CRC. Cochran's Q statistic and the inconsistency index (I2) were used to check study heterogeneity. Egger's test and funnel plots were applied to assess publication bias. All statistical analyses were conducted by with MetaAnalyst and MIX version 1.7. Results: Thirty four case-control studies involving a total of 9,143 cases and 11,357 controls were retrieved according to the inclusion criteria. Overall, no significant association was found between the MTHFR C677T polymorphism and colorectal cancer in Asian populations (for T vs. C: OR=1.03; 95% CI= 0.92-1.5; p= 0.64; for TT vs CC: OR=0.88; 95%CI= 0.74-1.04; p= 0.04; for CT vs. CC: OR = 1.02; 95%CI= 0.93-1.12; p=0.59; for TT+ CT vs. CC: OR=1.07; 95%CI= 0.94-1.22; p=0.87). Conclusions: Evidence from the current meta-analysis indicated that the C677T polymorphism is not associated with CRC risk in Asian populations. Further investigations are needed to offer better insight into any role of this polymorphism in colorectal carcinogenesis.

Molecular and biochemical characterization of hemoglobinase, a cysteine proteinase, in Paragonimus westermani

  • Choi Joon-Hyuck;Lee Jae-Hyuk;Yu Hak-Sun;Jeong Hae-Jin;Kim Jin;Hong Yeon-Chul;Kong Hyun-Hee;Chung Dong-Il
    • Parasites, Hosts and Diseases
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    • v.44 no.3
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    • pp.187-196
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    • 2006
  • The mammalian trematode Paragonimus westermani is a typical digenetic parasite, which can cause paragonimiasis in humans. Host tissues and blood cells are important sources of nutrients for development, growth and reproduction of P. westermani. In this study, a cDNA clone encoding a 47 kDa hemoglobinase of P. westermani was characterized by sequencing analysis, and its localization was investigated immunohistochemically. The phylogenetic tree prepared based on the hemoglobinase gene showed high homology with hemoglobinases of Fasciola hepatica and Schistosoma spp. Moreover, recombinant P. westermani hemoglobinase degradaded human hemoglobin at acidic pH (from 3.0 to 5.5) and its activity was almost completely inhibited by E-64, a cysteine proteinase inhibitor. Immunohistochemical studies showed that P. westermani hemoglobinase was localized in the epithelium of the adult worm intestine implying that the protein has a specific function. These observations suggest that hemoglobinase may act as a digestive enzyme for acquisition of nutrients from host hemoglobin. Further investigations may provide insights into hemoglobin catabolism in P. westermani.

Biochemical Analysis of Physiological Stress Induced by High Frequency Sound Treatment in the Beet Armyworm, Spodoptera exigua (고주파 처리에 따른 파밤나방(Spodoptera exigua)의 생리적 스트레스의 생화학적 분석)

  • Kim, Yong-Gyun;Son, Ye-Rim;Seo, Sam-Yeol;Park, Bok-Ri;Park, Jung-A
    • Korean journal of applied entomology
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    • v.51 no.3
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    • pp.255-263
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    • 2012
  • High frequency sounds disrupt physiological processes, such as feeding behavior, development and immune responses of Spodoptera exigua. We analyzed high frequency sounds with respect to biochemical changes in S. exigua. High frequency sound (5,000 Hz, 95 dB) suppressed protein synthesis and secretion of midgut epithelium. It also significantly inhibited a digestive enzyme activity of phospholipase $A_2$. The gene expression of three different heat shock proteins and apolipophorin III was altered, particularly in midgut tissue in response to high frequency sound treatments. High frequency sound treatments significantly increased sugar and lipid levels in hemolymph plasma. These results suggest that high frequency sounds are a physiological stress that induces biochemical changes in S. exigua.

Bioavailability of Phosphorus in Feeds of Plant Origin for Pigs - Review -

  • Weremko, D.;Fandrejewski, H.;Zebrowska, T.;Han, In K.;Kim, J.H.;Cho, W.T.
    • Asian-Australasian Journal of Animal Sciences
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    • v.10 no.6
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    • pp.551-566
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    • 1997
  • Phosphorus has been known as an essential component of animal body. However, the requirement has not been determined precisely because of the variable bioavailabilities of feedstuffs from plant origin. The bioavailability of P in various feedstuffs of plant origin varies from 10 to 60%. Digestibility and availability of the P differed considerably depending on the feed. The lowest values were found for maize (under 20%), the highest for wheat and triticale (over 50%). This is due to the proportion of phytate and the presence of intrinsic phytase. And the digestive tract of monogastric animals does not contain sufficient amounts of phytase, an enzyme that hydrolyses the unavailable phytate complexes to available, inorganic orthophosphates. Microbial phytase supplementation improves the P availability, and both intrinsic plant and microbial phytase improves the availability of P in feedstuffs of plant origin. In a mixture of feeds with low and high activity of intrinsic phytase and/or supplemented by commercial phytase, the P availability is additive. However, in the light of current results it seems that exceeding the P availability equal to 60-70% is unrealizable even at large microbial phytase doses.

Apparent Digestibility of Phosphorus in Experimental Feeds and the Effect of Commercial Phytase

  • Fandrejewski, H.;Raj, S.;Weremko, D.;Zebrowska, T.;Han, In K.;Kim, J.H.;Cho, W.T.
    • Asian-Australasian Journal of Animal Sciences
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    • v.10 no.6
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    • pp.665-670
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    • 1997
  • The digestibility (apparent) of P and other nutrients from the RSM, SBM and 2 batches of maize, wheat and barley was investigated in two experiments with 24 castrated male growing pigs. The effect of supplemental microbial phytase (1,000 U/kg) was also evaluated. The diets contained 25% RSM (Exp. 1) or 40% SBM (Exp. 2) and had no inorganic P. In each period of digestive trial, after 9 days of adaptation, faeces were collected for 5 days. The digestibility of P contained in the RSM and SBM was calculated by difference method. The P digestibility in maize, wheat, barley was on average 20, 34 and 36%, respectively. The digestibility of P in the RSM and SBM estimated from maize-based diets were 19 and 24 %, respectively. Kind of cereal grain had significant (p < 0.05) influence on the digestibility of P which was lower in the diets based on maize than wheat or barley. The digestibility of P significantly increased with the supplemental microbial phytase (on an average of 17%). Moreover, inclusion of enzyme into the diets positively affected digestibility of other nutrients, namely the protein and organic matter.

Effects of an Herbal Medicine, Gagam-daewhang mangcho-tang, and its Components on Cerulein-induced Acute Pancreatitis in Mice (加減大黃芒硝湯및 그 구성약재가 Cerulein으로 유도된 생쥐의 急性 膵臟炎에 미치는 影響)

  • Yu, Ju-yeon;Yu, Keun-jeong;Shin, Yong-jeen;Lee, Un-jung
    • The Journal of Internal Korean Medicine
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    • v.36 no.2
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    • pp.105-121
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    • 2015
  • Objectives: This study investigated the effects of Gagam-daewhang mangcho-tang (GDM) and its components on cerulein-induced acute pancreatitis (AP) in mice Methods: The AP mouse model was induced by intra-peritoneal injection of cerulein (50 μg/kg) at hourly intervals for 6 times. The experimental drug was administrated intraperitoneally 1 hour prior to the first injection of cerulein. Mice were sacrificed at 6 hours after the last injection of cerulein. Blood samples were taken to determine serum amylase level. The pancreas and lungs were rapidly removed for histochemical examination and myeloperoxidase (MPO) assays. Results: Administration of modified GDM significantly reduced the ratio of pancreas/body weight, level of serum amylase, neutrophil infiltration, and histological damage of the pancreas and lung. In a test of the components of GDM, the Salvia miltiorrhiza (SM) group showed a significant suppression of the severity of AP. In an experiment testing the concentration of SM, the 150 mg/kg SM group showed significant attenuation of the severity of AP. Conclusions: Modified GDM and a SM water extract could attenuate AP and AP-associated lung injury via suppression of digestive enzyme secretion and MPO activity.

Characterization of an Extracellular Lipase in Burkholderia sp. HY-10 Isolated from a Longicorn Beetle

  • Park, Doo-Sang;Oh, Hyun-Woo;Heo, Sun-Yeon;Jeong, Won-Jin;Shin, Dong-Ha;Bae, Kyung-Sook;Park, Ho-Yong
    • Journal of Microbiology
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    • v.45 no.5
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    • pp.409-417
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    • 2007
  • Burkholderia sp. HY-10 isolated from the digestive tracts of the longicorn beetle, Prionus insularis, produced an extracellular lipase with a molecular weight of 33.5 kDa estimated by SDS-PAGE. The lipase was purified from the culture supernatant to near electrophoretic homogenity by a one-step adsorption-desorption procedure using a polypropylene matrix followed by a concentration step. The purified lipase exhibited highest activities at pH 8.5 and $60^{\circ}C$. A broad range of lipase substrates, from $C_4\;to\;C_{18}$ p-nitrophenyl esters, were hydrolyzed efficiently by the lipase. The most efficient substrate was p-nitrophenyl caproate ($C_6$). A 2485 bp DNA fragment was isolated by PCR amplification and chromosomal walking which encoded two polypeptides of 364 and 346 amino acids, identified as a lipase and a lipase foldase, respectively. The N-terminal amino acid sequence of the purified lipase and nucleotide sequence analysis predicted that the precursor lipase was proteolytically modified through the secretion step and produced a catalytically active 33.5 kDa protein. The deduced amino acid sequence for the lipase shared extensive similarity with those of the lipase family 1.2 of lipases from other bacteria. The deduced amino acid sequence contained two Cystein residues forming a disulfide bond in the molecule and three, well-conserved amino acid residues, $Ser^{131},\;His^{330},\;and\;Asp^{308}$, which composed the catalytic triad of the enzyme.