• 제목/요약/키워드: Y-protein

검색결과 31,663건 처리시간 0.05초

The predictive value of serum myeloma protein in solitary plasmacytoma

  • Chang, Won Ick;Koh, Hyeon Kang;Yoon, Sung-Soo;Kim, Han-Soo;Eom, Keun-Yong;Kim, Il Han
    • Radiation Oncology Journal
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    • 제38권2호
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    • pp.129-137
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    • 2020
  • Purpose: To identify the clinical usefulness of serum M protein and to establish a rationale for regular follow-up with serum protein electrophoresis in solitary plasmacytoma. Materials and Methods: Sixty-nine patients with solitary plasmacytoma and solitary plasmacytoma with minimal marrow involvement according to the International Myeloma Working Group criteria were retrospectively reviewed. Results: At a median follow-up of 6.2 years, 5-year local control (LC), 5-year multiple myeloma-free survival (MMFS), 5-year failure-free survival (FFS), and 5-year overall survival (OS) were 82.6%, 44.1%, 41.8%, and 85.1%, respectively. Among the patients whose initial serum M protein was present or not evaluated, 37.3% of patients showed disappearance of serum M protein after various treatment. MMFS of these patients were comparable to non-secretory plasmacytoma with undetectable levels of M protein, and significantly better than patients with persistent M protein. Increase of serum M protein ≥0.1 g/dL was most predictive of treatment failure with area under the curve of 0.731. Conclusion: Patients who eventually showed persistence of serum M protein after treatment showed worse MMFS and FFS compared to those whose serum M protein disappeared or who had initially non-secretory disease. The increase of serum M protein level ≥0.1 g/dL from current nadir was predictive of treatment failure. Therefore, regular follow-up with serum M protein is highly recommended especially unless the patient had initially non-secretory disease.

Electrophoretic Mobility to Monitor Protein-Surfacant Interactions

  • Hong, Soon-Taek
    • Preventive Nutrition and Food Science
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    • 제3권2호
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    • pp.143-151
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    • 1998
  • Protein -surfactant interactions have been investigate by measuring ζ-potential of $\beta$-lactoglobulin-coated emulsion droplets and $\beta$-lactoglobulin in solution in the rpesenceof surfactant, with particular emphasis on the effect of protein heat treatment(7$0^{\circ}C$, 30min). When ionic surfactant (SDS or DATEM) is added to the protein solution, the ζ-potential of the mixture is found to increase with increasing surfactant concentration, indicating surfactant binding to the protein molecules. For heat-denatured protein,it has been observed that the ζ-potential tends to be lower than that of the native protein. The effect of surfactant on emulsions is rather complicated .With SDS, small amounts of surfactant addition induce a sharp increase in zeta potential arising from the specific interaction of surfactant with protein. With further surfacant addition, there is a gradual reductio in the ζ-potential, presumably caused by the displacement of adsorped protein (and protein-surfactant complex) from the emulsion droplet surfac by the excess of SDS molecules. At even higher surfactant concentrations, the measured zeta potential appears to increase slightly, possibly due to the formation of a surfactant measured zeta potential appears to increase slightly, possibly due to the formation of surfactant micellar structure at the oil droplet surface. This behaviour contrastswith the results of the corresponding systems containing the anionic emulsifier DATEM, in which the ζ-potential of the system is found to increase continuously with R, particularly at very low surfactant concentration. Overall, such behaviour is consisten with a combination of complexation and competitive displacement between surfactant and protein occurring at the oil-water interface. In addition, it has also been found that above the CMC, there is a time-dependent increase in the negative ζ-potential of emulsion droplets in solutions of SDS, possibly due to the solublization of oil droplets into surfactant micelles in the aqueous bulk phase.

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An evaluation of heat on protein oxidation of soy protein isolate or soy protein isolate mixed with soybean oil in vitro and its consequences on redox status of broilers at early age

  • Zhang, Xianglun;Lu, Peng;Xue, Wenyue;Wu, Dawei;Wen, Chao;Zhou, Yanmin
    • Asian-Australasian Journal of Animal Sciences
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    • 제30권8호
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    • pp.1135-1142
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    • 2017
  • Objective: The objective of this study was to evaluate effects of heat treatment and soybean oil inclusion on protein oxidation of soy protein isolate (SPI) and of oxidized protein on redox status of broilers at an early age. Methods: SPI mixed with soybean oil (SPIO) heated at $100^{\circ}C$ for 8 h was used to evaluate protein oxidation of SPI. A total of two hundred and sixteen 1-day-old Arbor Acres chicks were divided into 3 groups with 6 replicates of 12 birds, receiving basal diet (CON), heat-oxidized SPI diet (HSPI) or mixture of SPI and 2% soybean oil diet (HSPIO) for 21 d, respectively. Results: Increased protein carbonyl, decreased protein sulfhydryl of SPI were observed as heating time increased in all treatments (p<0.05). Addition of 2% soybean oil increased protein carbonyl of SPI at 8 h heating (p<0.05). Dietary HSPI and HSPIO decreased the average daily gain of broilers as compared with the CON (p<0.05). Broilers fed HSPI and HSPIO exhibited decreased glutathione (GSH) in serum, catalase activity and total sulfhydryl in liver and increased malondialdehyde (MDA) and protein carbonyl in serum, advanced oxidation protein products (AOPPs) in liver and protein carbonyl in jejunal mucosa as compared with that of the CON (p<0.05). Additionally, broilers receiving HSPIO showed decreased glutathione peroxidase activity (GSH-Px) in serum, GSH and hydroxyl radical scavenging capacity in liver, GSH-Px activity in duodenal mucosa, GSH-Px activity and superoxide anion radical scavenging capacity in jejunal mucosa and increased AOPPs in serum, MDA and protein carbonyl in liver, MDA and AOPPs in jejunal mucosa (p<0.05). Conclusion: Protein oxidation of SPI can be induced by heat and soybean oil and oxidized protein resulted in redox imbalance in broilers at an early age.

한국성인 여성의 단백질 섭취수준과 동.식물성 급원이 칼슘 및 인대사에 미치는 영향 (Effects of Dietary Protein Levels and Sources on Calcium and Phosphorus Metabolism in Young Korean Women)

  • 구재옥
    • Journal of Nutrition and Health
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    • 제24권2호
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    • pp.124-131
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    • 1991
  • 식이 단백질 섭취수준 및 동·식물성 단백질 급원이 칼슘 및 인대사에 미치는 영향을 검토하기 위하여 10명의 한국성인 연성을 대상으로 26일간의 통제 식이실험을 실시하였다. 대사실험 연구는 6일간의 적응기간과 10일간의 중단백식이(60g 단백질 545mg Ca)와 10일간의 고단백질 식이(90g 단백질 575mg Ca)로 구성되었다 중·고단백 식이기간 동안 동물성 단백질(75% 동물성 단백질)과 식물성 단백질(75% 식물성 단백질) 식이군으로 나누어 같은 식이에서 중단백식이 후 고단백식이를 섭취토록 하였고 실험식이 마지막 4일간은 각 2명에게 300mg 칼슘을 보충시켰다. 칼슘 흡수율은 단백질 섭취량의 증가시 동물성 단백질 식이군에서 유의적으로 증가하였다, 칼슘 보충은 급원에 관계없이 칼슘 흡수를 증가시켰다. 중단백 식이기간 동안 동물성과 단백질 식이에서 칼슘흡수율은 약 30% 이었으며 고단백질식이 기간 동안 동물성 단백질에서 46% 식물성 단백질에서 37% 이었다. 칼슘을 보충시켰을 때 중단백 식이기간동안 칼슘 흡수율은 약 46% 이었으며 고단백 식이군에서 53%이었다 뇨중 칼슘배설은 단백질 섭취수준에는 영향을 받지 않았으나 동물성 단백질 식이에서 식물성 단백질 식이보다 칼슘배설양이 많았다. 칼슘 균형을 단백질 섭취증가와 칼슘 보충으로 호전되었다. 인의 흡수는 단백질 섭취수준에는 영향을 받지않았으며 인 섭취량에 따라 증가하였다. 인 흡수율은 동물성 단백질 식이군에서 약 77∼81% 로 식물성 단백질 식이군에서의 55∼65% 보다 높았다. 이상의 결과로 보아 단백질 섭취수준 60g에서 90g으로의 증가와 칼슘보충은 뇨중 칼슘 배설에는 영향을 주지않으며 칼슘 흡수를 증진시켜 칼슘균형을 호전시키는 것으로 나타났다.

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Protein Evaluation of Dry Roasted Whole Faba Bean (Vicia faba) and Lupin Seeds (Lupinus albus) by the New Dutch Protein Evaluation System: the DVE/OEB System

  • Yu, P.;Egan, A.R.;Leury, B.J.
    • Asian-Australasian Journal of Animal Sciences
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    • 제12권6호
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    • pp.871-880
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    • 1999
  • The effects of dry roasting (110, 130, $150^{\circ}C$ for 15, 30, 45 min) on potential ruminant protein nutritional values in terms of: a), rumen bypass protein (BCP); b), rumen bypass starch (BST); c), fermented organic matter (FOM); d), true absorbed bypass protein (ABCP); e) microbial protein synthesized in the rumen based on available energy (E_MP); f), microbial protein synthesized in the rumen based on available nitrogen (N_MP); g), true protein supplied to the small intestine (TPSI); h), true absorbed rumen synthesized microbial protein (AMP); i), endogenous protein losses (ENDP); j), true digested protein in the small intestine (DVE); k), degraded protein balance (OEB) of whole lupin seeds (WLS) and faba beans (WFB) were evaluated by the new Dutch DV/OEB protein evaluation system. Dry roasting significantly increased BCP, BST, TPSI, ABCP, DVE (p<0.001) and decreased FOM, E_MP, AMP, N_MP and OEB (p<0.001) with increasing temperatures and times except that when temperature was at $110^{\circ}C$. The values of BCP, BST, TPSI, ABCP and DVE at $150^{\circ}C/45min$ for WLS and WFB were increased 2.2, 3.7; -, 2.0; 1.7, 1.7; 2.3, 3.7 and 1.7, 1.7 times and the values of FOM, E_MP, AMP, N_MP and OEB at $150^{\circ}C/45min$ for WLS and WFB were decreased by 15.3, 25.8; 18.1, 25.8; 18.7, 25.8; 54.6, 41.6 and 82.3% 54.7%, respectively, over the raw WLS and WFB. The results indicated that though dry roasting reduced microbial protein synthesis due to reducing FOM, TPSI didn't decrease but highly increased due to increasing BCP more than enough for compensation of the microbial protein decreasing. Therefore the net absorbable DVE in the small intestine was highly increased. The OEB values were significantly reduced for both WLS and WFB but not to the level of negative. It indicated that microbial protein synthesis might not be impaired due to the sufficient N supplied in the rumen, but the high positive OEB values in the most treatments except of $150^{\circ}C$ for 30 and 45 min of WLS (The OEB values: 54.8 and 26.0 g/kg DM) indicated that there were the large amounts of N loss in the rumen. It was concluded that dry roasting at high temperature was effective in shifting protein degradation from rumen to intestines and it increased the DVE values without reaching the negative OEB values. No optimal treatment was found in WLS due to the too high OEB values in all treatments. But dry roasting at $150^{\circ}C$ for 30 and 45 min might be optimal treatments for WLS due to the very lower OEB values.

쥐 소뇌에 있어서 raf protein kinases 의 면역세포 화학적 분포와 단백질 양상 (Immunocytochemical distribution of raf protein kinases and protein pattern in rat cerebellum)

  • 박정순;최원철
    • 생명과학회지
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    • 제8권1호
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    • pp.14-26
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    • 1998
  • 본 연구에서는 SDS/polyacrylamide 젤 전기영동에 의한 쥐의 성장과정에 따른 소뇌의 단백질양상의 변화양상과 immunocytochemistry를 이용하여 c-raf a-raf kinase의 정상 소뇌에서의 분포에 대해 관찰 하였으며 western blot을 이용하여 소뇌의 단백질들에서 c-raf의 존재에 대해 살펴보았다. 단백질 양상에서 쥐의 성장에 따라 crude에선,ㄴ 49,200 dalton과 169,000 dalton 사이의 bands가 양적 증가를 보였으며 cytosolic fraction 에서는 37,800 dalton의 band가 양적 증가를 보이는데 비해 membrane fraction 에서는 260,600 dalton의 band가 증가하였다. 이러한 결과로 성장 발달에 따라 고분자 량의 물질들이 이들 소뇌 부위에서 기여하였을 것으로 추정할 수 있었다. Immunocytochemistry에 의한 분석에서는 c-raf와 a-raf가 소뇌의 피질주위에서 조롱박 세포(Purkinje cell) 의 세포질 특히 핵 주변부위에서 강하게 검출되었으며 a-raf에 비해 c-raf가 더 강하게 나타났었다. 그리고 그 외에 Nucleus embolifornis의 큰 neuronal cell의 세포질 부위의 나타남을 볼 수 있었다. Immunoblot에 의한 분석에서는 crude와 cytosolic fraction에서 raf protein kinase의 존재를 확인할 수 있었으며, 이상의 결과들을 종합해 보았을 때 소뇌의 정상의 많은 신경세포(neuronal cell)에 raf protein kinase가 분포되어 있으며 이들이 정상의 cell에서 기능을 가질 것으로 추정된다.

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야생 호밀 염색체 첨가 밀 계통의 단백질 발현 양상 비교 분석 (Identification of the Protein Function and Comparison of the Protein Expression Patterns of Wheat Addition Lines with Wild Rye Chromosomes)

  • 이대한;조건;우선희;조성우
    • 한국작물학회지
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    • 제64권4호
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    • pp.373-383
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    • 2019
  • 야생 호밀 염색체 첨가 계통의 단백질 발현 양상을 보통 밀과 비교함으로써 발현의 차이를 보이는 단백질의 기능을 동정함으로써 야생 호밀의 작물학적 유용 가치를 확인하고자 이 연구를 수행하였다. 전반적으로 야생 호밀 염색체 첨가계통은 보통 밀의 유전적 배경을 바탕으로 건조와 열에 대한 비생물학적 스트레스에 대한 저항성 관련 단백질과 바이러스성 병원균에 대한 저항성 관련 단백질 및 척박한 환경에 적응하는 생리대사에 관련된 단백질을 가지고 있는 것을 확인하였다. 하지만 아직 야생 호밀의 단백질 기능에 대한 정보와 작물학적 이용에 대한 연구가 미흡한 상태이다. 앞으로 국내 야생 호밀의 유용 유전자원으로써의 작물학적 이용과 기능에 대한 지속적인 연구가 필요하다.

Ruminal Protein Degradation Characteristics of Cell Mass from Lysine Production

  • Seo, S.;Kim, H.J.;Lee, S.Y.;Ha, Jong K.
    • Asian-Australasian Journal of Animal Sciences
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    • 제21권3호
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    • pp.364-370
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    • 2008
  • Chemical analysis and in vitro studies were conducted to investigate the nutritive value for ruminants of cell mass from lysine production (CMLP) which is a by-product of the lysine manufacturing process. Proximate analysis, protein fractionation, and in vitro protein degradation using protease from Streptomyces griseus and strained ruminal fluid were carried out to estimate ruminal protein degradability of CMLP with two reference feedstuffs-soybean meal (SBM) and fish meal (FM). Amino acid composition and pepsin-HCl degradability were also determined to evaluate postruminal availability. CMLP contained 67.8% crude protein with a major portion being soluble form (45.4% CP) which was composed of mainly ammonium nitrogen (81.8% soluble CP). The amount of nucleic acids was low (1.15% DM). The total amount of amino acids contained in CMLP was 40.60% DM, which was lower than SBM (47.69% DM) or FM (54.08% DM). CMLP was composed of mainly fraction A and fraction B2, while the protein fraction in SBM was mostly B2 and FM contained high proportions of B2 and B3 fractions. The proportion of B3 fraction, slowly degradable protein, in CP was the highest in fish meal (23.34%), followed by CMLP (7.68%) and SBM (1.46%). CMLP was degraded up to 51.40% at 18 h of incubation with Streptomyces protease, which was low compared to FM (55.23%) and SBM (83.01%). This may be due to the insoluble portion of CMLP protein being hardly degradable by the protease. The in vitro fermentation by strained ruminal fluid showed that the amount of soluble fraction was larger in CMLP (40.6%) than in SBM (17.8%). However, because the degradation rate constant of the potentially degradable fraction of CMLP (2.0%/h) was lower than that of SBM (5.8%/h), the effective ruminal protein degradability of CMLP (46.95%) was slightly lower than SBM (53.77%). Unavailable fraction in the rumen was higher in CMLP (34.0%) compared to SBM (8.8%). In vitro CP degradability of CMLP by pepsin was 80.37%, which was lower than SBM (94.42%) and FM (89.04%). The evaluation of protein degradability using different approaches indicated that soluble protein in CMLP may supply a large amount of ammonia in the rumen while insoluble protein can be by-passed from microbial attacks due to its low degradability. The results from this study suggest that CMLP can be used as a protein supplement to ruminants for supplying both non-protein nitrogen to rumen microbes and rumen undegradable protein to the host animal.

Effect of Protein Sources on Rumen Microbial Protein Synthesis Using Rumen Simulated Continuous Culture System

  • Joo, J.W.;Bae, G.S.;Min, W.K.;Choi, H.S.;Maeng, W.J.;Chung, Y.H.;Chang, M.B.
    • Asian-Australasian Journal of Animal Sciences
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    • 제18권3호
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    • pp.326-331
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    • 2005
  • A rumen simulated continuous culture (RSCC) system was used to study the influence of supplementation of the three different types of protein sources such as urea, casein and soy protein on rumen microbial synthesis in terms of rumen microbial synchronization. The urea treatment showed the highest pH value. Ammonia nitrogen concentration was rapidly increased after feeding and not significantly different in the urea treatment (13.53 mg/100 ml). Protozoa numbers were not significantly different for soy protein and casein treatment compared to urea treatments during incubation. The average concentration of total VFA (mMol) was not detected with significant difference among treatments, but iso-butyrate production showed the highest for soy protein treatment among treatments (p<0.001). The lowest concentration in total iso-acids (iso-butyrate and iso-valerate) production was observed in urea treatment. The soy protein treatment showed no significantly change in acetate/propionate. The amounts of dry matter (DM) out flow showed no significant difference among treatments. Organic matter (OM) flow was the highest for urea treatments and the lowest for casein treatment (p<0.03). The nitrogen flow for casein treatment was not significantly different from other treatments. The efficiency of microbial protein synthesis in terms of microbial nitrogen (MN) synthesis (g MN/kg ADOM) digested in the rumen was highest for casein treatment (58.53 g MN/kg ADOM) compared to soy protein and urea (p<0.05). This result suggests that rumen ammonia releasing rate may influence on microbial protein synthesis in the rumen.

Influence of Protein and Energy Level in Finishing Diets for Feedlot Hair Lambs: Growth Performance, Dietary Energetics and Carcass Characteristics

  • Rios-Rincon, F.G.;Estrada-Angulo, A.;Plascencia, A.;Lopez-Soto, M.A.;Castro-Perez, B.I.;Portillo-Loera, J.J.;Robles-Estrada, J.C.;Calderon-Cortes, J.F.;Davila-Ramos, H.
    • Asian-Australasian Journal of Animal Sciences
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    • 제27권1호
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    • pp.55-61
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    • 2014
  • Forty-eight Pelibuey${\times}$Katahdin male intact lambs ($23.87{\pm}2.84$ kg) were used in an 84-d feeding trial, with six pens per treatment in a $2{\times}2$ factorial design arrangement. The aim of the study was to evaluate the interaction of two dietary energy levels (3.05 and 2.83 Mcal/kg ME) and two dietary protein levels (17.5% and 14.5%) on growth performance, dietary energetics and carcass traits. The dietary treatments used were: i) High protein-high energy (HP-HE); ii) High protein-low energy (HP-LE); iii) Low protein-high energy (LP-HE), and iv) Low protein-low energy (LP-LE). With a high-energy level, dry matter intake (DMI) values were 6.1% lower in the low-protein diets, while with low-energy, the DMI values did not differ between the dietary protein levels. Energy levels did not influence the final weight and average daily gain (ADG), but resulted in lower DMI values and higher gain efficiencies. No effects of protein level were detected on growth performance. The observed dietary net energy (NE) ratio and observed DMI were closer than expected in all treatments and were not affected by the different treatments. There was an interaction (p<0.03) between energy and protein level for kidney-pelvic and heart fat (KPH), KPH was higher in lambs fed high energy and high protein diet but not in high energy and low protein diet. The KPH was increased (20.2%, p = 0.01) in high-energy diets, while fat thickness was increased (21.7%, p = 0.02) in high-protein diets. Therefore, it is concluded that dietary energy levels play a more important role in feed efficiency than protein levels in finishing lambs with a high-energy diet (>2.80 Mcal/kg ME). Providing a level of protein above 14.5% does not improves growth-performance, dietary energetics or carcass dressing percentage.