• 한국가금학회지
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• 제45권2호
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• pp.73-79
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• 2018

본 연구의 주제는 대체원료를 옥수수와 대두박을 대신해 첨가될 때의 원료가격들의 변화와 대체원료의 적정한 가격을 판단할 수 있는 방법을 제시하는 것이다. 옥수수과 대두박 그리고 대체원료의 가격 변화는 각각의 원료사료들의 영양소 함량과 가격 및 대체원료의 첨가량을 바탕으로 계산된다. 원료사료의 가격 변화 계산에 필요한 각 원료사료들의 대체가는 대체원료를 사용함으로써 새로 추가되거나 제외되는 영양소의 함량들을 %로 표현한 것을 의미한다. 본 계산에서 사료가격의 순변화는 질소보정 외관상 대사에너지(Nitrogen-corrected apparent metabolizable energy), 표준회장가소화(Standardized ileal digestible) 라이신(Lys), 메티오닌(Met), 트레오닌(Thr) 및 트립토판(Trp) 그리고 총 칼슘(Total Ca)과 가용인(Available P) 함량을 바탕으로 계산하였다. 계산 결과, 옥수수주정박 단위무게당 새로 첨가되거나 제외되는 원료사료들의 함량에 대한 방정식은 다음과 같다: 1 ${\times}$ 옥수수주정박 + 0.0334 ${\times}$ 대두유 + 0.0182 ${\times}$ 석회석 = 0.8893 ${\times}$ 옥수수 + 0.13 ${\times}$ 대두박 + 0.0004 ${\times}$ 라이신 + 0.0022 ${\times}$ 메티오닌 + 0.0005 ${\times}$ 트립토판 + 0.0028 ${\times}$ 트레오닌 + 0.0264 ${\times}$ 제2인산칼슘 위 식과 원료사료들의 가격을 이용하여 옥수수주정박을 각 원료사료의 에너지와 영양소함량을 고려하여 15% 정도 옥수수와 대두박을 대체시 옥수수주정박의 가격은 270원/kg으로 계산되었다. 결론적으로 본 연구에서 이용한 엑셀기반 계산 프로그램은 육계 사료에서 대체원료의 경제적 가치를 판단할 때에 도움이 될 수 있을 것으로 사료된다.

• 한국양식학회지
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• 제15권3호
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• pp.157-163
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• 2002

본 실험은 섭취촉진물질로 알려져 있는 사료내 13종의 아미노산들이 치어기 조피볼락에 있어 성장 및 체조성에 어떠한 영향을 미치는지 알아보고자 실시하였다 실험어는 평균무게 0.64 g인 조피볼락 치어를 사용하였으며, 기초실험 사료내에 유인효과가 있을 것으로 여겨지는 아미노산 13가지(Arg, Ala, Na-Glu, Gly, His, Ile, Lys, Met, Phe, Pro, Thr, Trp 및 Val)를 사료내 각각 0.3% 씩 첨가하여 총 13 실험구를 2반복으로 나누어 6주간 사육하였다. 6주간의 사육실험 결과, 성장률(WG)과 일간 성장률(SGR)에서는 Pro, Thr, Met 및 Gly 실험구가 다른 실험구에 비해 유의적으로 높았으나(P<0.05), 이들 실험구간에는 유의적인 차이가 없었다(P>0.05). 그리고, 사료전환효율(FE)에서는 Pro 실험구가 Met과 Gly 실험구보다 유의적으로 높았으며(P<0.05), Pro 실험구와 Thr 실험구 사이에는 유의적인 차이가 없었다(P>0.05). 그리고 Thr, Met 및 Gly 실험구간에도 유의적인 차이가 없었다(P>0.05). 단백질전화효율에 있어서 Pro 실험구가 모든 실험구에 있어서 유의적으로 가장 높았으며(P<0.05), Thr 실험구와 비교하여 유의적으로 차이가 나지 않았다(P>0.05). 그리고, 비만도(condition factor)는 Thr 실험구가 유의적으로 가장 높았으며(P<0.05), Val 실험구는 가장 낮게 나타났다(P>0.05). 간중량지수(HSI)는 모든 실험구간에서 유의적인 차이가 나지 않았다(P>0.05). 전어체의 단백질, 수분 및 회분에 있어서는 모든 실험구에 있어서 유의적인 차이가 나지 않았다(P>0.05). 지질함량은 Met, Pro 및 Thr 실험구가 Glu, Gly, Lys, Trp 및 Val 실험구보다 유의적으로 낮았다(P>0.05). 상기 결과를 토대로, 조피볼락 사료용 사료섭취촉진물질로서 아미노산을 검색한 결과 사료내 0.3% Pro, Thr, Met 및 Gly을 첨가했을 때 사료섭취촉진 효과가 나타났으며, 이것들 중 Gly을 제외하고는 전어체의 지질 함량을 감소시키는 결과를 나타내었다.

• 생명과학회지
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• 제12권1호
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• pp.96-105
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• 2002

식물 단백질의 영양가 향상을 위한 일환으로 필수아미노산의 조성이 풍부한 인공단백질을 암호화하는 인공유전자를 담배 식물체에서 발현을 시도하기 위하여, 식물에서 외래유전자의 발현에 널리 사용되는 Cauliflower mosaic virus (CaMV)의 35S promoter를 이중으로 중첩되도록 하고, (Lys-Glu-Trp)이 64번 반복되는 인공유전자 및 nopaline synthase (nos) terminator를 갖고있는 binary vector pART4-4를 구성하였다. 이 재조합 플라스미드는 Agrobacterium tumefaciens를 이용한 형질전환에 의해 Nicotiann tabacum (Var. Xanthi)으로 도입되었다. Kanamycin이 포함된 신초 유도 배지 및 뿌리 유도배지를 이용하여 정상적으로 재생된 담배 식물체로부터 도입된 인공유전자의 발현을 분석하였다. 추출한 genomic DNA를 EcoRI으로 자른 다음 Southern blot 분석에 의하면, 효소 절단 시 예상되는 1.1 kb에서 band를 형성하였으며 각각의 형질전환 식물체에 인공유전자가 1 또는 3 개씩 도입되어 있음을 확인하였다. Northern blot 분석에 의하면 약 1.2 kb 전사체가 비교적 안정하게 발현되었으며, 잎, 줄기, 뿌리로부터 RNA를 분리하여 promoter의 조직 특이성 발현을 분석한 결과, 잎에서 생성되는 RNA가 줄기나 뿌리 조직보다 안정하게 발현되었다. 형질전환 식물체에서 Western blot에 의한 단백질 분석 결과, 잎에서 추출한 단백질로부터 원하는 크기인 33 kDa의 인공단백질이 생성됨을 확인하였으며 발현 수준은 전체 세포 단백질의 0.1%로서 낮은 수준이었다.

• Animal Bioscience
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• 제36권4호
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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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• 제37권8호
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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.

• 방사선산업학회지
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• 제7권2_3호
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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.

• 한국식물병리학회:학술대회논문집
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• 한국식물병리학회 2005년도 한국식물병리학회 임시총회 및 춘계학술발표회
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• pp.50.2-51
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• 2005

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 1995년도 제3회 추계심포지움
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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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• 제9권2호
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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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• 제28권1호
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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.