• Title/Summary/Keyword: 단백질 강성

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Protein-Protein Interaction Reliability Enhancement System based on Feature Selection and Classification Technique (특징 추출과 분석 기법에 기반한 단백질 상호작용 데이터 신뢰도 향상 시스템)

  • Lee, Min-Su;Park, Seung-Soo;Lee, Sang-Ho;Yong, Hwan-Seung;Kang, Sung-Hee
    • The KIPS Transactions:PartB
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    • v.13B no.7 s.110
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    • pp.679-688
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    • 2006
  • Protein-protein interaction data obtained from high-throughput experiments includes high false positives. In this paper, we introduce a new protein-protein interaction reliability verification system. The proposed system integrates various biological features related with protein-protein interactions, and then selects the most relevant and informative features among them using a feature selection method. To assess the reliability of each protein-protein interaction data, the system construct a classifier that can distinguish true interacting protein pairs from noisy protein-protein interaction data based on the selected biological evidences using a classification technique. Since the performance of feature selection methods and classification techniques depends heavily upon characteristics of data, we performed rigorous comparative analysis of various feature selection methods and classification techniques to obtain optimal performance of our system. Experimental results show that the combination of feature selection method and classification algorithms provide very powerful tools in distinguishing true interacting protein pairs from noisy protein-protein interaction dataset. Also, we investigated the effects on performances of feature selection methods and classification techniques in the proposed protein interaction verification system.

Production and Characterization of Monoclonal Antibodies Specific to PAT Protein Expressed in Genetically Modified Herbicide-Resistance Maize (제초제 내성 유전자 변형 옥수수 중 PAT단백질에 특이한 단크론성 항체의 생산과 특성 확인)

  • Kim, Sol-A;Lee, Jeong-Eun;Shim, Won-Bo;Kang, Sung-Jo;Chung, Duck-Hwa
    • Journal of Food Hygiene and Safety
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    • v.33 no.3
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    • pp.193-199
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    • 2018
  • In this study, PAT protein of genetically modified maize was prepared from the recombinant E. coli strain BL21 (DE3), and mice were immunized with the recombinant PAT protein. After cell fusion and cloning, two hybridoma cells (PATmAb-7 and PATmAb-12) were chosen since the monoclonal antibodies (Mabs) produced by them were confirmed to be specific to PAT protein in the indirect enzyme-linked immunsorbent assay (ELISA) and western blot tests. There were no cross-reactions of either Mabs to other GM proteins or to the extracts of non-GM maize. The ELISA based on the PATmAb-7 can sensitively detect 0.3 ng/g PAT protein in corn. These results indicate that the developed Mabs can be used as bio-receptors in the development of immunosensors and biosensors for the rapid and simple detection of GM corn adulterated in foods.

Simple Sequence Repeat Markers Linked to Quantitative Trait Loci Controlling Seed Weight, Protein and Oil Contents in Soybean (콩에서 종실의 무게와 oil 및 단백질 함량을 조절하는 양적 형질 유전자좌와 연관된 simple sequence repeat marker)

  • Kim, Hyeun-Kyeung;Kang, Sung-Taeg;Choung, Myoung-Gun;Jung, Chan-Sik;Oh, Ki-Won;Baek, In-Youl;Son, Beung-Gu
    • Journal of Life Science
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    • v.16 no.6
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    • pp.949-954
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    • 2006
  • Soybean [Glycine max (L.) Merr.] is an important crop, accounting for 48% of the world market in oil crops. Improvement of the quality and quantity of soybean seed constituents is one of the most important objectives in soybean breeding. Protein content and seed size are important properties to determine the quality of tofu and soy sprouts respectively. The objective of this study was to identify quantitative trait loci (QTLs) that control seed weight, protein and oil content in soybean. The 117 $F_{2:10}$ recombinant inbred lines (RlL) developed from a cross of 'Keunolkong' and 'Shinpaldalkong' were used. Narrow-sense heritability estimates based on a plot mean on seed weight, protein and oil content were 0.8, 0.78 and 0.71, respectively. Four independent QTLs for seed weight were identified from linkage group (LG) F, I and K. Five QTL for protein content were located on LG D1b, E, H, I and L. Oil content was related with six QTLs located on LG D1b, E, G, I, J and N. Protein and oil content have three common QTLs on LG D1b, E and I. Thus, we identified major loci improving soybean seed quality.

High-level Expression of Human Procaspase-9 in Escherichia coli and Purification of its GST-tagged Recombinant Protein (대장균을 이용한 세포사멸 유도 단백질 caspase-9의 발현에 관한 연구)

  • Seong, Yeong-Mo;Han, Cheol;Choe, Ju-Yeon;Park, Hyo-Jin;Seong, Geun-Hye;Nam, Min-Gyeong;Kim, Sang-Su;Kim, In-Gyeong;Gang, Seong-Man;Im, Hyang-Suk
    • Korean Journal of Microbiology
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    • v.39 no.4
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    • pp.216-222
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    • 2003
  • Human caspase-9, an essential apoptosis initiator protease, was excessively degraded when expressed in Escherichia coli under the conventional induction condition. To optimize the conditions for induction and develop a rapid purification method for obtaining significant amounts of wild-type procaspase-9, we expressed procaspase-9 as GST fusion in E. coli. The addition of 0.01 mM IPTG as an inducer to the bacterial culture and decreasing the culture temperature to 25oC improved the production of procasapse-9 protein by circumventing proteolytic degradation in E. coli. The wild-type procaspae-9 was purified to approximately 70% purity with relatively high yields using the method developed in this study. In addition, we found that GST-caspase-9 is autocatalytically cleaved after aspartic acid 315, which is the same site for processing in mammalian cells, during expression in E. coli.

Characterization of Azospirillum spp. Isolated from Korean Paddy Roots (우리나라 수도근권에서 분리된 Azospirillum spp.의 특성)

  • 조무제;강규영;강성모;윤한대
    • Korean Journal of Microbiology
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    • v.25 no.2
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    • pp.129-136
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    • 1987
  • Nitrogen fixing activity associated with 40 varieties of rice was assayed at heading stage by an in situ acetylene reduction method. The in situ acetylene reduction activity and population of nitrogen fixing bacteria obtained on nitrogen-free malate medium for Azospirillum spp. enrichment showed positive correlation. Six Azospirillum spp. with high nitrogenase activity were isolated from the rice roots, from which five spp. were identified as A. lipoferum and one was A. brasilense. The physiological characteristics of the six Azospirillum isolates, that is, carbon source utilization, biotin requirement, antibiotic resistance, indole acetic acid excretion, plasmid profile and protein patterns were compared.

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Recovery of Soy Oligosaccharides using Calcium Oxide (산화칼슘을 이용한 대두 올리고당의 회수)

  • Choi, Yeon-Bae;Kim, Kang-Sung;Sohn, Heon-Soo
    • Korean Journal of Food Science and Technology
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    • v.27 no.2
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    • pp.225-229
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    • 1995
  • Soy oligosaccharide, a low calorie sugar, which is known to improve the intestinal microbial flora, was recovered from the waste of soymilk process by Steffen process. To remove protein contaminants, prior to the Steffen process, pH of the sample was adjusted to $3.5{\sim}4.0$ or calcium chloride was added 8%(w/w) per sugar. Both pretreatment processes were found to remove about $25{\sim}30%$ of the protein initially present in the sample. Using the Steffen process, as much as 85% of soy oligosaccharide could be recovered as a saccharate form. The amounts of calcium chloride and lime used were 20%(w/w) and $100{\sim}120%$(w/w) per total sugar, respectively. After the sugar was desorbed by $CO_{2}$, the final yield of oligosaccharide was 80% while 80% of protein were removed from the original solution. The composition of sugar was similar to that of soybean cooking water.

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Selective Removal of Protease from Soybean Cell Wall Degrading Enzyme Complex Isolated from Aspergillus niger CF-34 (Aspergillus niger CF-34로부터 분리한 대두세포벽분해효소 복합체 중의 Protease의 선택적인 제거)

  • Choi, Yeon-Bae;Kim, Kang-Sung;Sohn, Heon-Soo
    • Korean Journal of Food Science and Technology
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    • v.27 no.3
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    • pp.370-374
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    • 1995
  • By exposing the complex enzyme solution to alkaline condition, it was possible to remove the protease activity selectively without inactivation of soybean cell wall degrading activity of the crude enzyme complex produced by Aspergillus niger CF-34. Optimum reaction conditions were as follow. pH was $9.0{\pm}0.1$, temperature was $20^{\circ}C$ and reaction time was 30 min with gentle stirring. Over 90% of protease activity could be eliminated while the activities of pectinase, polygalacturonase, xylanase, carboxymethyl cellulase and soybean cell wall degrading enzyme were maintained to $80{\sim}100%$. Through alkali treatment, it was discovered that the quality and organoleptic properties of soy protein produced by this enzymes were improved because the hydrolysis of protein and formation of bitter peptide were decreased.

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