• Title/Summary/Keyword: Trypsin inhibitor

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Roasting and Extruding Affect Nutrient Utilization from Soybeans in 5 and 10 kg Nursery Pigs

  • Kim, I.H.;Hancock, J.D.;Hines, R.H.;Gugle, T.L.
    • Asian-Australasian Journal of Animal Sciences
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    • v.13 no.2
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    • pp.200-206
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    • 2000
  • Ninety nursery pigs were used in two metabolism experiments to determine the effects of roasting and extruding on the nutritional value of Williams 82 soybeans with (+K) and without (-K) gene expression for the Kunitz trypsin inhibitor. Treatments for both experiments were: 1) soybean meal; 2) +K roasted; 3) +K extruded; 4) -K roasted; and 5) -K extruded. Diets were the soybean preparations (96.5% of the diet) with only vitamins and minerals added as needed to meet or exceed NRC recommendations. Daily feed allowance was 5% of initial BW given as three equal meals. In Exp. 1, 50 weanling pigs (4.7 kg average BW and 21 d average age) were used. Apparent values for N digestibility (p<0.001), biological value (p<0.09), percentage N retention (p<0.05), GE digestibility (p<0.001) and percentage ME (p<0.001) were greater for pigs fed extruded soybeans than pigs fed roasted soybeans. Also, N digestibility (p<0.05), biological value (p<0.03) and percentage N retention (p<0.04) were greater for pigs fed -K soybeans than those fed +K soybeans. In Exp. 2, 40 pigs (9.7 kg average BW and 35 d average age) were allowed to adjust to the nursery environment before use in the experiment. In general, the pigs in Exp. 2 (i.e., the older pigs) had greater utilization of nutrients from all of the soybean products than the younger pigs used in Exp. 1. Digestibilities of DM, N and GE were greater (p<0.001) for pigs fed -K soybeans than those fed +K soybeans and extruded soybeans had greater digestibilities of DM, N and GE than roasted soybeans (p<0.001). Also, percentage N retention (p<0.01) and percentage ME (p<0.001) for pigs fed extruded soybeans were greater than for pigs fed roasted soybeans. In conclusion, extruded and -K soybeans were greater nutritional value than roasted and +K soybeans for 4.7 and 9.7 kg nursery pigs.

Effects of Ulinastatin on Postoperative Blood Loss and Hemostasis in Atrioventricular Valve Surgery with Cardiopulmonary Bypass

  • Park, Jae Bum;Kim, Seong Hyop;Lee, Song Am;Chung, Jin Woo;Kim, Jun Seok;Chee, Hyun Keun
    • Journal of Chest Surgery
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    • v.46 no.3
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    • pp.185-191
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    • 2013
  • Background: Cardiopulmonary bypass (CPB) induces variable systemic inflammatory reactions associated with major organ dysfunction via polymorphonuclear neutrophils (PMNs). Ulinastatin, a urinary trypsin inhibitor, inhibits PMN activity and reduces systemic inflammatory responses. The aim of this study is to evaluate the effect of ulinastatin on postoperative blood loss and laboratory changes in patients undergoing open heart surgery. Materials and Methods: Between January 2008 and February 2009, 110 patients who underwent atrioventricular valve surgery through right thoracotomy were divided into two groups. Patients received either 5,000 U/kg ulinastatin (ulinastatin group, n=41) or the equivalent volume of normal saline (control group, n=69) before aortic cross clamping. The primary end points were early coagulation profile changes, postoperative blood loss, transfusion requirements, and duration of intubation and intensive care unit stay. Results: There were no statistically significant differences between the two groups in early coagulation profile, other perioperative laboratory data, and postoperative blood loss with transfusion requirements. Conclusion: Administration of ulinastatin during operation did not improve the early coagulation profile, postoperative blood loss, or transfusion requirements of patients undergoing open heart surgery. In addition, no significant effect of ulinastatin was observed in major organs dysfunction, systemic inflammatory reactions, or other postoperative profiles.

Treatments Effect on Biological Values of Defatted Rice Polishings

  • Khalique, Anjum;Lone, K.P.;Khan, A.D.;Pasha, T.N.
    • Asian-Australasian Journal of Animal Sciences
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    • v.19 no.2
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    • pp.209-216
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    • 2006
  • Defatted rice polishings (DRP) was subjected to chemical treatments i.e., 0.4 N HCl, and 6% $H_2O_2$, with or without physical treatment i.e. extrusion cooking. The treated DRP was evaluated chemically and biologically using male broiler chicks (108) of approximately uniform weight, selected out of 220 chicks, previously fed on commercial diets for 7 days as a settlement period. The chicks were then divided into 36 experimental units of 3 chicks each. Each experimental diet was randomly allotted to three experimental units and fed for 10 days to broiler chicks. The experimental diets were designated as A (Commercial), B (10% HCl treated DRP), C (20% HCl treated DRP), D (10% HCl plus extruded DRP), E (20% HCl plus extruded DRP), F (10% $H_2O_2$ DRP) and G (20% $H_2O_2$ DRP), H (10% $H_2O_2$ plus extrusion DRP) and I (20% $H_2O_2$ plus extrusion DRP), J (10% untreated DRP), K (20% untreated DRP) and L (Protein free). The birds fed on diet L were used to measure the endogenous nitrogen loss. The biological evaluations of diets containing differently treated DRP were compared with a commercial feed and feeds containing untreated defatted rice polishings. It was observed that these treatments liberated bound nutrients, making them more accessible to the normal digestive enzymes and increased their apparent nutrient availability. This process probably also detoxified the anti-nutritive factors i.e. phytates, lectin, trypsin inhibitor present in DRP. The results of the feeding trials revealed that diets containing 6% $H_2O_2$ treated DRP showed better weight gain, feed consumption and utilization, protein efficiency and digestibility, biological value and net protein utilization than all other treatments.

An Infant Case of Citrin Deficiency with Corresponding Biochemical Features and a Heterozygous SLC25A13 Mutation (SLC25A13 이형접합 유전자 변이와 부합하는 생화학적 소견을 가진 영아 시트린 결핍증 1례)

  • Kang, Su Min;Chi, Yang Hyun;Lee, Jun Hwa
    • Journal of The Korean Society of Inherited Metabolic disease
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    • v.15 no.3
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    • pp.155-159
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    • 2015
  • Citrin deficiency (OMIN #605814) is an autosomal recessive disorder caused by the SLC25A13 gene mutation with abnormal biochemical findings, including increased serum ammonia, citrulline, arginine, galactose, serum threonine-to-serine ratio, serum pancreatic secretory trypsin inhibitor, and alpha-fetoprotein. Citrin deficiency can manifest in three ways: in newborns as neonatal intrahepatic cholestasis caused by citrin deficiency (NICCD), in older children as failure to thrive and dyslipidemia caused by citrin deficiency (FTTDCD), and in adults as citrullinemia type 2 (CTLN2) with recurrent hyperammonemia and neuropsychiatric symptoms. We report a 35-day-old asymptomatic patient with citrin deficiency who had abnormal biochemical findings.

Development of a thrombolytic agent from Korean snake venums (한국 독사독으로부터 혈전 용해제 개발에 관한 연구)

  • Lee, Moon-Han;Kim, Byung-Jae;Lee, Hang;Ryu, Pan-Dong;Cho, Myung-Haeng;Lee, Hye-Sook;Kim, Jong-Ho;Chae, Chang-Soo
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1995.04a
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    • pp.114-114
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    • 1995
  • 이 연구에서는 혈전증 치료에 사용되는 혈전 응해제를 국내 독사독으로부터 개발하기 위한 실험을 실시하였다. 그 내용을 요약하면 다음과 같다. 국내에 서식하는 독사인 Agkistrodon blomoffi brevicaudus, Agkistrodon caliginosus와 Agkistrodon saxatilis에서 각각 사독을 채취하여 fibrin plate 방법으로 fibrin 분해능을 조사하여 Agkistrodon blomoffi brevicaudus의 독이 분해능이 가장 우수함을 밝혔다. 이와 같은 사실에 기초하여 A. blomoffi brevicaudus의 독으로부터 p-Aminobenzamidine affinity chromatography와 DEAE ion-exchange chromatography를 이용하여 분자량이 50.8 kDa인 황성 단백질을 정제하였다. 위에서와 같은 방법으로 정제한 단백질은 fibrin 분해능이 우수하고 fibrinogen의 ${\gamma}$ chain은 분해하지 않으나 B$\beta$ chain을 $A\alpha$ chain에 비하여 보다 선택적으로 분해하는 단백분해 효소임을 증명하였다. 이 정제 효소의 Fibrin에 대한 분해능은 266$\mu\textrm{g}$/${\mu}\ell$의 농도에서 Plasmin 1.0 unit (=3.0 WHO unit)보다 높게 나타났다. 정제된 효소는 chromogenic substrate인 N-Benzoyl-Phe-Val-Arg-pNA와 N-p-Tosyl- Gly-Pro-Arg-pNA의 arginine carboxyl side를 분해하고 pH 7.5에서 최대 활성을 보이며, Vmax는 5.46 umo1/1ㆍmin이고, Km 값은 0.20mM이며, 그리고 Cu$^{2+}$, $Zn^{2+}$, soybean trypsin inhibtor에 의해 25~50% 정도, serine proteinase inhibitor인 phenylmethylsulfonyl floride에 의해 80%정도 활성이 억제되는 특성이 있음을 규명하였다.

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[ $\beta$ ]-Secretase (BACE1) Inhibitors from Sanguisorbae Radix

  • Lee, Hee-Ju;Seong, Yeon-Hee;Bae, Ki-Hwan;Kwon, Soon-Ho;Kwak, Hye-Min;Nho, Si-Kab;Kim, Kyung-A;Hur, Jong-Moon;Lee, Kyung-Bok;Kang, Young-Hwa;Song, Kyung-Sik
    • Archives of Pharmacal Research
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    • v.28 no.7
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    • pp.799-803
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    • 2005
  • In the course of screening anti-dementia agents from natural products, two $\beta$-secretase (BACE1) inhibitors were isolated from the ethyl acetate soluble fraction of Sanguisorbae Radix by the activity-guided purification using silica gel, Sephadex LH-20, and RP-HPLC. They were identified as 1,2,3-trigalloyl-4,6-hexahydroxydiphenoyl-$\beta$-D-glucopyranoside (Tellimagrandin II, 1) and 1,2,3,4,6-pentagalloyl-$\beta$-D-glucopyranoside (2) and were shown to non-competitively inhibit $\beta$-secretase (BACE1) with the $IC_{50}$ values of $3.10{\times}10^{-6}M\;and\;3.76{\times}10^{-6}M$, respectively. The Ki values of 1 and 2 were $6.84{\times}10^{-6}M\;and\;5.13{\times}10^{-6}M$. They were less inhibitory to asecretase (TACE) and other serine proteases such as chymotrypsin, trypsin, and elastase, suggesting that they were relatively specific inhibitors of BACE1.

Purification and Characterization of a Serine Protease (CPM-2) with Fibrinolytic Activity from the Dung Beetles

  • Ahn, Mi-Young;Hahn, Bum-Soo;Ryu, Kang-Sun;Hwang, Jae-Sam;Kim, Yeong-Shik
    • Archives of Pharmacal Research
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    • v.28 no.7
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    • pp.816-822
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    • 2005
  • Catharsius protease-2 (CPM-2) was isolated from the body of dung beetles, Catharsius molossus, using a three step purification process (ammonium sulfate fractionation, gel filtration on Bio-Gel P-60, and affinity chromatography on DEAE Affi-Gel blue). The purified CPM-2, having a molecular weight of 24 kDa, was assessed homogeneously by SDS-polyacrylamide gel electrophoresis. The N-terminal amino acid sequence of CPM-2 was composed of X Val Gin Asp Phe Val Glu Glu lie Leu. CPM-2 was inactivated by $Cu^{2+}\;and\;Zn^{2+}$ and strongly inhibited by typical serine proteinase inhibitors such as TLCK, soybean trypsin inhibitor, aprotinin, benzamidine, and ${\alpha}_1$-antitrypsin. However, EDTA, EGTA, cysteine, $\beta$-mercaptoethanol, E64, and elastatinal had little effect on enzyme activity. In addition, antiplasmin and antithrombin III were not sensitive to CPM-2. Based on the results of a fibrinolytic activity test, CPM-2 readily cleaved $A{\alpha}-$ and $B{\beta}$-chains of fibrinogen and fibrin, and y-chain of fibrinogen more slowly. The nonspecific action of the enzyme resulted in extensive hydrolysis, releasing a variety of fibrinopeptides of fibrinogen and fibrin. Polyclonal antibodies of CPM-2 were reactive to the native form of antigen. The ELISA was applied to detect quantities, in nanograms, of the antigen in CPM-2 protein.

Plant Phenolics as ${\beta}$-Secretase (BACE1) Inhibitors

  • Jun, Mi-Ra;Lee, Seung-Ho;Choi, Sun-Ha;Bae, Ki-Hwan;Seong, Yeon-Hee;Lee, Kyung-Bok;Song, Kyung-Sik
    • Food Science and Biotechnology
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    • v.15 no.4
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    • pp.617-624
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    • 2006
  • Various plant phenolics were assessed for (${\beta}$-secretase (BACE1) inhibitory activity in order to screen for anti-dementia agents. Among 39 phenolics, eight compounds, 1,2,3-trigalloyl glucopyranoside, acetonyl geraniin, euphorscopin, furosine, helioscopinin A, helioscopinin B, jolkinin, and rugosin E exhibited strong inhibition of BACE1 with $IC_{50}$ values of $5.87{\times}10^{-8}-54.93{\times}10^{-6}\;M$. Among them, rugosin E was the most potent ($IC_{50}$ $5.87{\times}10^{-8}\;M$). The active compounds were shown to be non-competitive inhibitors by Dixon plot. All the phenolic BACE1 inhibitors except furosin also suppressed prolyl endopeptidase (PEP) activity. However, these phenolic compounds caused less inhibition of ${\alpha}$-secretase (tumor necrosis factor a converting enzyme; TACE) and no significant inhibition of other serine proteases such as trypsin, chymotrypsin, and elastase was seen, demonstrating that they are relatively specific to both BACE1 and PEP. No significant structure-activity relationships were found.

Inheritance between Le Gene and Ti Gene in Soybean (Glycine max L.)

  • Lee, Kyoung Ja;Park, Mo Se;Sung, Mi Kyung;Kim, Myung Sik;Chung, Jong Il
    • Korean Journal of Breeding Science
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    • v.40 no.2
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    • pp.97-100
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    • 2008
  • Lectin protein and Kunitz trypsin inhibitor (KTI) protein of mature soybean seed are a main antinutritional factor in soybean seed. The Le gene controls a lectin protein and Ti gene controls the KTI protein in soybean. Ti locus has been located on linkage group 9 in the classical linkage map of soybean. Position of Le locus on linkage map was not identified. Genetic relationship between Ti locus and Le locus could be useful in soybean breeding program for the genetic elimination of these factors. The objective of this study was to determine the independent inheritance or linkage between Ti locus and Le locus in soybean seed. Two $F_2$ populations were developed from three parents (Gaechuck#1, T102, and PI548415). The $F_1$ seeds from Gaechuck#1 (titiLeLe) ${\times}$ T102 (TiTilele) and Gaechuck#1 (titiLeLe) ${\times}$ PI548415 (TiTilele) were obtained. The lectin and KTI protein were analysed from $F_2$ seeds harvested from the $F_1$ plants to find independent assortment or linkage between Ti locus and Le locus. The segregation ratios of 3 : 1 for Le locus (129 Le_ : 44 lele) and Ti locus (132 Ti_ : 41 titi) and were observed. The segregation ratios of 9 : 3 : 3 : 1 (95 Le_Li_ : 34 Le_titi: 37 leleTi_ : 7 leletiti) between Le gene and Ti gene in $F_2$ seeds were observed. This data showed that Ti gene was inherited independently with the Le gene in soybean. These results will be helpful in breeding program for selecting the line with lacking both KTI and lectin protein in soybean.

Serum concentrations of α2-macroglobulin, α1-antitrypsin, and C-reactive protein in dogs with suspected acute pancreatitis

  • Park, Soyoung;Kim, Hakhyun;Kang, Ji-Houn;Kang, Byeong-Teck;Yang, Mhan-Pyo
    • Korean Journal of Veterinary Research
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    • v.59 no.1
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    • pp.9-15
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    • 2019
  • In canine acute pancreatitis (AP), inappropriate release and activation of zymogen proteases within the pancreas results in the consumption of serum antiproteases. The aim of this study was to examine whether the serum concentrations of ${\alpha}_2$-macroglobulin (A2MG), ${\alpha}_1$-antitrypsin (A1AT), and C-reactive protein (CRP) differ between dogs with AP and healthy dogs. Twenty healthy dogs and 20 dogs with AP were included in this study. Concentrations of A2MG, A1AT, and CRP were measured in the sera of healthy dogs and dogs diagnosed with AP. Serum A2MG and A1AT concentrations were significantly lower in dogs with AP than in healthy dogs, whereas the serum CRP concentration was significantly higher. In addition, the concentrations of A2MG and A1AT were significantly higher in AP survivors than in AP non-survivors, while the CRP concentration was significantly lower. However, in both AP survivors and non-survivors, the CRP concentrations showed a negative correlation with A2MG concentrations but not with A1AT. These findings indicate that serum antiproteases and CRP concentrations might be associated with the mortality rate of AP in dogs.