• Korean Journal of Poultry Science
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• v.45 no.2
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• pp.73-79
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• 2018

The objective of this study was to calculate the unit price of an alternative feed ingredient for broiler chickens in consideration of the energy and nutritive contents in the feed ingredient by using a simple Excel worksheet. A corn-distiller's dried grains with solubles (corn-DDGS) was used as an alternative ingredient and corn and soybean meal as ingredients to be replaced. The net change of feed price was calculated based on the replacement values which were estimated in consideration of energy and nutrient concentration in feed ingredients used in the calculation, the price of feed ingredients and inclusion rate of the alternative ingredient. The nitrogen corrected apparent metabolizable energy(AMEn) and standardized ileal digestible AA including Lys, Met, Thr, and Trp, total Ca, and available P were employed as nutritive component to calculate the replacement values for individual feed ingredients. The equation for replacement was 1 ${\times}$ corn-DDGS + 0.0334 ${\times}$ soybean oil + 0.0182 ${\times}$ Limestone = 0.8893 ${\times}$ corn + 0.13 ${\times}$ soybean meal + 0.0004 ${\times}$ Lys + 0.0022 ${\times}$ Met + 0.0005 ${\times}$ Trp + 0.0028 ${\times}$ Thr + 0.0264 ${\times}$ dicalcium phosphate. The replacement price of corn-DDGS was calculated to be 270 won/kg when the inclusion rate was 15% and the energy and nutrient contents were considered in the calculation. In conclusion, the Excel-based ingredient price calculator may be useful to determine the economic value when an alternative feed ingredient is used in diets fed to broiler chickens.

• Journal of Aquaculture
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• v.15 no.3
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• pp.157-163
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• 2002

Thirteen groups, each consisting of 25 juveniles (0.64 g) of the Korean rockfish, Sebastes schlegeli were reared in aquaria after period of one week conditioning. Each group was fed with one of the 13 diets at the rate of 7~10% body weight (on a dry-matter basis) 2 times a day for 6 weeks. Each diet was supplemented with one of the following amino acids at 3g/kg diet: Alanine (Ala), Arginine (Arg), Glycine(Gly), Glutamate (Glu), Histidine (His), Isoleusine(Ile), Lysine (Lys), Methionine (Met), Phenylalanine (Phe), Proline (Pro), Threonine (Thr), Tryptophan (Trp) or Valine (Val). Groups fed with Pro, Thr, Met or Gly-supplemented diet showed significantly (p<0.05) higher weight gain and faster specific growth rate than the groups fed on other diets, while those fed Pro, Thr, Met or Gly were not significantly different each other(P>0.05). Feed efficiency (FE) of fish fed Pro was significantly higher than those fed the other diets except that fed Thr (P<0.05). However, there was no significant difference between FE of fish fed Pro and Thr, and among FE of fish fed Thr, Met and Gly (P>0.05). The requirement of rockfish is higher for Met and Thr. Extra Pro and/or Gly may also stimulate biosynthesis of the nucleic acids (IMP, GMP) which are known as the feed stimulant in fish.

• Journal of Life Science
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• v.12 no.1
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• pp.96-105
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• 2002

To investigate expression of the artificial gene encoding a repeated tripeptide lysyl-glutamyl-tryptophan in tobacco plant, the plant binary vector, pART404 has been constructed, which contains the duplicated CaMV 35S promoter, an artificial gene coding for repetitive polymer (Lys-Glu-Trp)$_{64}$, and nopaline synthase (nos) terminator. The recombinant expression vector was introduced in Nicotiana tabacum (var. Xanthi) via Agrobacterium tumefaciens-mediated trans-formation. The transgenic calli selected by kanamycin containing medium were then regenerated to whole plants. Southern blot analysis indicated that five transgenic plants (No. 1, 7, 9, 43, 45) showed the hybridizing signals at 1.1 kb of the expected size on EcoRI digestion and each of the transgenic plants contained 1 or 3 copies of the artificial gene inserted into its genome. By northern blot analysis, the size of the hybridized total RNA was estimated to be approximately 1.2 kb and the RNA appeared generally to have the integrity. Western blot indicated that the protein was detected at the position of 33 kDa and the expression level of the polypeptide in the transgenic plant (No. 45) was measured to approximately 0.1% of the total protein.

• Animal Bioscience
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• v.36 no.4
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• pp.619-628
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• 2023

Objective: This study aimed to determine and compare the apparent ileal digestibility (AID) and the standardized ileal digestibility (SID) of amino acids (AA) in soybean meal (SBM), cottonseed meal (CSM), and low-gossypol cottonseed meal (LCSM) fed to broiler chickens and laying hens. Methods: Three semi-purified diets containing the identical crude protein concentration at 20% were formulated to contain SBM, CSM, or LCSM as the sole source of N. A N-free diet was also formulated to estimate the basal ileal endogenous losses of AA for broilers and hens. A total of 300 male Ross 308 chicks at one-day-old and 144 Hy-Line Brown laying hens at 30-week-old with initial egg production rate of 88.3%±1.0% were randomly allocated into 1 of 4 dietary treatments, respectively. Results: CSM and LCSM showed more Arg and Cys+Met while less Lys, Ile, Leu, and Thr relative to SBM. Significant interactions existed between species and experimental diets for AID (except for Arg, Asp, Glu, Gly, and Pro) and SID (except for Arg, His, and Phe) of most AA. Most AA in diets showed higher AID (except for Lys) and SID (except for Lys, Met, and Ser) in broilers relative to laying hens. The AID and SID of all AA were significantly different between the three diets. In broilers, the AID and SID of most indispensable AA except for Arg in SBM and LCSM was higher than CSM. In laying hens, the AID and SID of most indispensable AA except for Arg, Met+Cys, and Phe in SBM was higher than CSM and LCSM. Conclusion: The accurate determination of AID and SID of AA in CSM and LCSM for broilers and layers benefits the application of CSM and LCSM in chicken diets. The cottonseed by-products CSM or LCSM showed the species-specific AA digestibility values for broilers and layers.

• Animal Bioscience
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• v.37 no.8
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• pp.1474-1482
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• 2024

Objective: The experiment aimed to determine the standardized ileal digestibility (SID) of crude protein (CP) and amino acids (AA) in 10 brown rice samples fed to pigs, and to construct predictive models for SID of CP and AA based on the physical characteristics and chemical composition of brown rice. Methods: Twenty-two cannulated pigs (initial body weight: 42.0±1.2 kg) were assigned to a replicated 11×3 incomplete Latin square design, including an N-free diet and 10 brown rice diets. Each period included 5 d adaptation and 2 d ileal digesta collection. Chromic oxide was added at 0.3% to all the diets as an indigestible marker for calculating the ileal CP and AA digestibility. Results: The coefficients of variation of all detected indices for physical characteristics and chemical composition, except for bulk weight, dry matter (DM) and gross energy, in 10 brown rice samples were greater than 10%. The SID of CP, lysine (Lys), methionine, threonine (Thr), and tryptophan (Trp) in brown rice was 77.2% (62.6% to 85.5%), 87.5% (80.3% to 94.3%), 89.2% (78.9% to 98.9%), 55.4% (46.1% to 67.6%) and 92.5% (86.3% to 96.3%), respectively. The best prediction equations for the SID of CP, Lys, Thr, and Trp were as following, SID_CP = -664.181+8.484×DM (R² = 0.40), SID_Lys = 53.126+6.031×ether extract (EE)+0.893×thousand-kernel volume (R² = 0.66), SID_Thr = 39.916+7.843×EE (R² = 0.41), and SID_Trp = -361.588+4.891×DM+0.387×total starch (R² = 0.85). Conclusion: Overall, a great variation exists among 10 sources of brown rice, and the thousand-grain volume, DM, EE, and total starch can be used as the key predictors for SID of CP and AA.

• Journal of Radiation Industry
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• v.7 no.2_3
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• pp.191-200
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• 2013

In this study, a novel bombesin (BBN) analogues, DOTA-Ala($SO_3H$)-4 aminobenzoyl-Gln-Trp-Ala-Val-Gly-His-Leu-Met-$NH_2$ (DOTA-sBBN) and DOTA-Lys(glucose)-4 aminobenzoyl-Gln-Trp-Ala-Val-Gly-His-Leu-Met-$NH_2$ (DOTA-gluBBN), were synthesized and radiolabeled, and their binding affinities were evaluated. Peptides were prepared by a solid phase synthesis method and their purities were over 98%. DOTA is the chelating agent for $^{177}Lu$-labeling, and the DOTA-conjugated peptides were radiolabeled with $^{177}Lu$ by a high radiolabeling yield (>98%). The Log P values of DOTA-sBBN and DOTA-gluBBN were -2.20 and -2.79, respectively. 50.41% of $^{177}Lu$-DOTA-sBBN and 72.97% of $^{177}Lu$-DOTA-gluBBN were left undegraded by the serum incubation at $37^{\circ}C$ for 48 hr. A competitive displacement of $^{125}I-[Tyr^4]$-BBN on the PC-3 human prostate carcinoma cells revealed that 50% inhibitory concentration ($IC_{50}$) were 1.46 nM of DOTA-sBBN and 4.67 nM of DOTA-gluBBN indicating a highly nanomolar binding affinity for GRPR. Therefore, it is concluded that $^{177}Lu$-DOTA-sBBN and $^{177}Lu$-DOTA-gluBBN can be potential candidates as a targeting modality for the Gastrin-releasing peptide receptor (GRPR)-over-expressing tumors, and further studies to evaluate their biological and pharmacological characteristics are needed.

• Proceedings of the Korean Society of Plant Pathology Conference
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• 2005.04a
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• pp.50.2-51
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• 2005

• Proceedings of the Korean Society of Applied Pharmacology
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• 1995.10a
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• pp.39-40
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• 1995

Thymopoietin(TP) was originally isolated from bovine thymic extracts on the basis of its ability to affect neuromuscular transmission when injected into mice (Goldstein, 1974). A 49 amino acid polypeptide was isolated and sequenced (Schlesinger and Goldstein, 1975). It is now evident that this molecule was created by proteolytic cleavage of larger thymopoietin proteins during isolation, and represents the N-terminal sequence of these proteins. Nevertheless, this proteolytic fragment was active in both neurophysiological and immunological experiments, and enabled the identification of an active pentapeptide. (amino acids 32 to 36, Arg-Lys-Asp-Val-Tyr, thymopentin), which. has been studied as an immunomodulatory drug.

• Journal of Photoscience
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• v.9 no.2
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• pp.255-257
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• 2002

In birds, the photoperiodic seasonal breeding involves encephalic photoreception at the initial step of triggering the well-known endocrinal cascade. Especially in Japanese quail (Coturnix coturnixjaponica), the reproductive neuroendocrine function responds to a single long day, and hypothalamic regions are known to be important for the reproductive response. However, little is known about where and how the light and time signals are integrated to detect daylength information and transduced to the endocrinal responses. To gain insights into this issue, we are interested in the c-Fos expression in the hypothalamus of the Japanese quail. Meddle and Follett (1997) previously identified two hypothalamic regions where c-Fos-like immunoreactivities were induced in response to a long day by using an antibody to carboxyl terminal region of human c-Fos (Lys$^{347}$ -Leu$^{367}$ ). In the present study, we used a different anti-c-Fos antibody recognizing a region from Lys$^{128}$ to Ala$^{152}$ of human c-Fos, and found in long-day- stimulated quails many c-Fos-like immunoreactive nuclei localizing within two regions, nucleus anterior medialis hypothalami and nucleus periventricularis hypothalami, which are distinct from those identified in the previous study. Then, we focused on the difference in the cross-reactivities of the antibodies used, and determined the whole coding sequence of quail c-Fos to compare the antigenic sequences of the two antibodies with the amino acid sequence of quail c-Fos. We found that the antibody we used would recognize quail c-Fos more specifically than that used in the previous study.

• BMB Reports
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• v.28 no.1
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• pp.72-78
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• 1995

Time-dependent inactivation of E. coli GTP cyclohydrolase I with a 2',3'-dialdehyde derivative of GTP (oGTP) was directed to the active site of the enzyme, and was dependent on the concentration of oGTP. The kinetics of inactivation were biphasic with a rapid reaction occurring immediately upon exposure of the enzyme to oGTP followed by a slow rate of inactivation. The $K_i$ value of oGTP for the enzyme was 0.25 mM. Inactivation was prevented by preincubation of the enzyme with GTP, the substrate of the enzyme. At 100% inactivation, 2.3 mol of [8.5'-$^3H$]oGTP were bound per each enzyme subunit, which consists of two identical polypeptides. The active site residue which reacted with the affinity label was lysine. oGTP interacted selectively with the ${\varepsilon}$-amino group of lysine in the GTP-binding site to form a morpholine-like structure which was stable without sodium borohydride treatment. However, triphosphate group was eliminated during the hydrolysis step. To identify the active site of the enzyme, [8.5'-$^3H$]oGTP-labeled enzyme was cleaved by endoproteinase Lys-C, and the $^3H$-labeled peptide was purified by HPLC. The amino acid sequence of the active site peptide was Pro-Ser-Leu-Ser-Lys, which corresponds to the aminoterminal sequence of the enzyme.