WordNet
- a process that uses heat to separate a substance into its components (同)fractional process
- separation into portions
- any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
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- 蛋白(たんばく)質
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- 1. 血漿分画製剤および組換えDNA産生凝固因子 plasma derivatives and recombinant dna produced coagulation factors
- 2. 免疫学的輸血反応 immunologic blood transfusion reactions
English Journal
- Molecular spectroscopic investigation on fractionation-induced changes on biomacromolecule of co-products from bioethanol processing to explore protein metabolism in ruminants.
- Zhang X1, Yan X2, Beltranena E3, Yu P4.Author information 1Department of Animal Science, Tianjin Agricultural University, Tianjin 300384, China; Department of Animal and Poultry Science, College of Agriculture and Bioresources, University of Saskatchewan, Saskatoon, SK S7N 5A8, Canada.2Department of Animal and Poultry Science, College of Agriculture and Bioresources, University of Saskatchewan, Saskatoon, SK S7N 5A8, Canada; The Branch Academy of Animal Science, Jilin Academy of Agricultural Science, Gongzhuling, Jilin 136100, China.3Research and Innovation Division, Alberta Agriculture and Rural Development, Edmonton, AB T6H 5T6, Canada.4Department of Animal Science, Tianjin Agricultural University, Tianjin 300384, China; Department of Animal and Poultry Science, College of Agriculture and Bioresources, University of Saskatchewan, Saskatoon, SK S7N 5A8, Canada. Electronic address: peiqiang.yu@usask.ca.AbstractFractionation processing is an efficient technology which is capable to redesign/redevelop a new food or feed product with a specified chemical and nutrient profile. This processing technique was able to produce four different fractions (called "A", "B", "C", "D" fractions/treatments) with different nutrient profile form a co-product of bioethanol processing [wheat dried distillers grains with soluble (DDGS)]. To date, there is no study on the effect of fractionation processing on inherent molecular structure of different fractions and how the processing-induced structural change affect the metabolic characteristics of protein and nutrient availability. The objectives of this experiment were to: (1) investigate the effect of fractionation processing on changes of protein functional groups (amide I, amide II, and their ratio) and molecular structure (modeled α-helix, β-sheet, and their ratio), and (2) study the relationship between the fractionation processing-induced changes of protein molecular structure and nutrients availability as well as the metabolic characteristics of protein. The hypothesis of this study was that the fractionation processing changes the molecular structure and such changes affect the metabolic characteristics of protein. The protein molecular structure spectral profile of the fractions A, B, C and D were identified by Fourier-transform infrared attenuated total reflection spectroscopy (FT/IR-ATR). The results showed that the fractionation processing significantly affected the protein molecular spectral profiles. The differences in amide I to amide II peak area and height ratios were strongly significant (P<0.01) among the treatment fractions, ranging from 4.98 to 6.33 and 3.28 to 4.00, respectively. The difference in the modeled protein α-helix to β-sheet ratio was also strongly significant (P<0.01) among the treatment fractions. Multivariate molecular spectral analysis with cluster (CLA) and principal component analyses (PCA) showed that there are no clear distinguished clusters and ellipses among the fractions (A, B, C and D) in the protein amide I and II region ca. 1726-1485cm(-1). The correlation study showed that the modeled α-helix to β-sheet ratio tended to have a negative correlation with truly absorbed rumen undegraded protein (ARUP(DVE): r=-0.944, P=0.056<0.10) and total truly absorbed protein in the small intestine (DVE: r=-0.946, P=0.054<0.10), but there was no correlation between the α-helix to β-sheet ratio and the degraded protein balance (DPB(OEB): P=0.267<0.10). In conclusion, the fractionation processing changed the molecular structural spectral profiles in terms of amide I to II ratio and α-helix to β-sheet ratio. These changes negatively affected the metabolic characteristics of protein and true protein supply. These results indicated that spectral features of different fractions could be used as a potential tool to predict true protein nutritive value.
- Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy.Spectrochim Acta A Mol Biomol Spectrosc.2014 Mar 25;122:591-7. doi: 10.1016/j.saa.2013.11.081. Epub 2013 Nov 21.
- Fractionation processing is an efficient technology which is capable to redesign/redevelop a new food or feed product with a specified chemical and nutrient profile. This processing technique was able to produce four different fractions (called "A", "B", "C", "D" fractions/treatments) with different
- PMID 24334060
- Chemical characteristics and fractionation of proteins from Moringa oleifera Lam. leaves.
- Teixeira EM, Carvalho MR, Neves VA, Silva MA, Arantes-Pereira L.Author information Department of Food and Nutrition, São Paulo State University, Araraquara, São Paulo, Brazil. Electronic address: estelamar@iftm.edu.br.AbstractMoringa oleifera Lam. is a leguminous plant, originally from Asia, which is cultivated in Brazil because of its low production cost. Although some people have used this plant as food, there is little information about its chemical and nutritional characteristics. The objective of this study was to characterise the leaves of M. oleifera in terms of their chemical composition, protein fractions obtained by solubility in different systems and also to assess their nutritional quality and presence of bioactive substances. The whole leaf flour contained 28.7% crude protein, 7.1% fat, 10.9% ashes, 44.4% carbohydrate and 3.0mg 100g(-1) calcium and 103.1mg 100g(-1) iron. The protein profile revealed levels of 3.1% albumin, 0.3% globulins, 2.2% prolamin, 3.5% glutelin and 70.1% insoluble proteins. The hydrolysis of the protein from leaf flour employing sodium dodecyl sulfate (SDS) and 2-mercaptoethanol (ME) resulted in 39.5% and 29.5%, respectively. The total protein showed low in vitro digestibility (31.8%). The antinutritional substances tested were tannins (20.7 mg g(-1)), trypsin inhibitor (1.45TIU mg g(-1)), nitrate (17 mg g(-1)) and oxalic acid (10.5 mg g(-1)), besides the absence of cyanogenic compounds. β-Carotene and lutein stood out as major carotenoids, with concentrations of 161.0 and 47.0 μg g(-1) leaf, respectively. Although M. oleifera leaves contain considerable amount of crude protein, this is mostly insoluble and has low in vitro digestibility, even after heat treatment and chemical attack. In vivo studies are needed to better assess the use of this leaf as a protein source in human feed.
- Food chemistry.Food Chem.2014 Mar 15;147:51-4. doi: 10.1016/j.foodchem.2013.09.135. Epub 2013 Oct 3.
- Moringa oleifera Lam. is a leguminous plant, originally from Asia, which is cultivated in Brazil because of its low production cost. Although some people have used this plant as food, there is little information about its chemical and nutritional characteristics. The objective of this study was to c
- PMID 24206684
- A comparison of the character of algal extracellular versus cellular organic matter produced by cyanobacterium, diatom and green alga.
- Pivokonsky M1, Safarikova J2, Baresova M2, Pivokonska L3, Kopecka I2.Author information 1Institute of Hydrodynamics, Academy of Sciences of the Czech Republic, Pod Patankou 5, 166 12 Prague 6, Czech Republic. Electronic address: pivo@ih.cas.cz.2Institute of Hydrodynamics, Academy of Sciences of the Czech Republic, Pod Patankou 5, 166 12 Prague 6, Czech Republic; Institute of Environmental Studies, Faculty of Science, Charles University, Benatska 2, 128 01 Prague 2, Czech Republic.3Institute of Hydrodynamics, Academy of Sciences of the Czech Republic, Pod Patankou 5, 166 12 Prague 6, Czech Republic.AbstractThis study investigated characteristics of algal organic matter (AOM) derived from three species (cyanobacterium Microcystis aeruginosa, diatom Fragilaria crotonensis and green alga Chlamydomonas geitleri) which dominate phytoplanktonic populations in reservoirs supplying drinking water treatment plants. Algal growth was monitored by cell counting, optical density and dissolved organic carbon concentration measurements. Extracellular organic matter (EOM) released at exponential and stationary growth phases and cellular organic matter (COM) were characterised in terms of specific UV absorbance (SUVA), peptide/protein and non-peptide content, hydrophobicity and molecular weight (MW). It was found that both EOM and COM were predominantly hydrophilic with low SUVA. COM was richer in peptides/proteins, more hydrophilic (with about 89% of hydrophilic fraction for all three species) and had lower SUVA than EOM. MW fractionation showed that both EOM and COM of all three species contain large portions of low-MW (<1 kDa) compounds and high-MW (>100 kDa) polysaccharides. Peptides/proteins exhibited narrower MW distribution than non-peptide fraction and it widened as the cultures grew. The highest amount of peptides/proteins with a significant portion of high-MW ones (22%) was observed in COM of M. aeruginosa. The results imply that the knowledge of AOM composition and characteristics predetermine which processes would be effective in the treatment of AOM laden water.
- Water research.Water Res.2014 Mar 15;51:37-46. doi: 10.1016/j.watres.2013.12.022. Epub 2013 Dec 24.
- This study investigated characteristics of algal organic matter (AOM) derived from three species (cyanobacterium Microcystis aeruginosa, diatom Fragilaria crotonensis and green alga Chlamydomonas geitleri) which dominate phytoplanktonic populations in reservoirs supplying drinking water treatment pl
- PMID 24388829
Japanese Journal
- トキイロヒラタケ色素成分の特徴
- 白坂 憲章,山口 裕加,吉岡 早香 [他],福田 泰久,寺下 隆夫
- 日本きのこ学会誌 : mushroom science and biotechnology 20(3), 147-153, 2012-10-31
- トキイロヒラタケ子実体よりピンク色と黄色の色素を分離した.ピンクの色素は,硫安塩析,DEAEトヨパール,トヨパールHW55によるクロマトグラフィーにより色素タンパク質として精製され,分子量はSDS-PAGEおよびHPLC-GPCによって,それぞれ24.5kDa,30kDaと推定された.本色素タンパクは267,348,493nmに吸収極大を示し,28℃およびpH4から10で安定であった.一方,黄色色 …
- NAID 110009553917
- Isolation, identification, and biological evaluation of Nrf2-ARE activator from the leaves of green perilla (Perilla frutescens var. crispa f. viridis)
- Izumi Yasuhiko,Matsumura Atsuko,Wakita Seiko,Akagi Ken-Ichi,Fukuda Hiroyuki,Kume Toshiaki,Irie Kazuhiro,Takada-Takatori Yuki,Sugimoto Hachiro,Hashimoto Tadashi,Akaike Akinori
- Free radical biology & medicine 53(4), 669-679, 2012-06-27
- … We isolated the active fraction from green perilla extract through bioactivity-guided fractionation. … Inhibition of the p38 mitogen-activated protein kinase pathway abolished ARE activation, the induction of γ-GCS and NQO1, and the cytoprotective effect brought about by DDC. …
- NAID 120004462161
- Characterization of Protein-like Fluorophores Released from Lake Phytoplankton on the Basis of Fractionation and Electrophoresis
- YAMADA Etsu,HIROTA Takaaki,HATORI Naoko [他],KITAO Yuki,FUSE Yasuro,AOKI Shinichi,KARATANI Hajime,MATSUNAGA Toshiro
- Analytical sciences : the international journal of the Japan Society for Analytical Chemistry 28(6), 595-600, 2012-06-10
- NAID 10030758052
Related Links
- Subcellular Protein Fractionation Kit 細胞成分ごとにタンパク質を分画抽出するキット 哺乳動物の培養細胞から、細胞質タンパク質・膜タンパク質・水溶性核タンパク質・クロマチン結合タンパク質・細胞骨格タンパク質のそれぞれに ...
- View kits, reagents and equipment for quick protein fractionation by physical properties or cellular location. Improve identification of low-abundance proteins. ... Life Science Research Products Amplification / PCR Flow Cytometry
Related Pictures
★リンクテーブル★
| リンク元 | 「蛋白分画」 |
| 関連記事 | 「fractionation」 |
「蛋白分画」
- 表：(血漿蛋白)LAB.473 「蛋白分画.xls」
概念
- 血清蛋白は電気泳動法により分画すると、易動度の大きい順にアルブミン、α1、α2、β, γグロブリンの5分画に分かれる。これらの分画が蛋白分画と呼ばれる？
Alb
- アルブミン(67kDa)
α1分画
α2分画
β分画
β-γ分画
- 血漿蛋白分画では出現する。
- フィブリノゲン：334kDa
γ分画
血漿蛋白分画
- LAB.474
| 分画 | 蛋白質 | 分子量 |
| プレアルブミン | トランスサイレチン | 55 kDa |
| アルブミン | アルブミン | 66.5 kDa |
| α1 | α1-酸性糖タンパク | 40 kDa |
| α1-アンチトリプシン | 54 kDa | |
| α1-リポ蛋白 | 13-36x10^4 kDa | |
| Gc-グロブリン | 54 kDa | |
| α1-α2 | セルロプラスミン | 132 kDa |
| α2 | α2-マクログロブリン | 725 kDa |
| ハプトグロビン | 100-400kDa | |
| pre βリポ蛋白(VLDL) | 19.6x10^6 kDa | |
| β | βリポ蛋白(LDL) | 2-3x10^6 kDa |
| トランスフェリン | 79.6 kDa | |
| ヘモペキシン | 57 kDa | |
| C3 | 180 kDa | |
| C4 | 210 kDa | |
| β～γ | フィブリノゲン | 334 kDa |
| γ | IgG | 160 kDa |
| IgA | 160 kDa | |
| SIgA(2IgA+SC+J) | 385 kDa | |
| IgM | 971 kDa | |
| CRP | ～120kDa |
- アルブミンは負に荷電しているのでよく泳動される
基準値
| 泳動の方向 | 分画 | 出典不明 | 2007年後期血液 | 覚えやすく | |
| ＋ | アルブミン | 60.5-73.2% | 4.9- 5.1 g/dL | 60-70% | 65% |
| ↑ | α1グロブリン | 1.7-2.9% | 0.11-0.23 g/dL | 2-3% | 2.5% |
| ↑ | α2グロブリン | 5.3-8.8% | 0.38-0.73 g/dL | 5-10% | 7.5% |
| ↑ | βグロブリン | 6.4-10.4% | 0.58-0.62 g/dL | 7-12% | 10% |
| － | γグロブリン | 11-21.1% | 1.15-1.25 g/dL | 10-20% | 15% |
疾患と蛋白分画の変化
- 鉄欠乏性貧血：β↑(トランスフェリン)
- ネフローゼ症候群：Alb↓(アルブミンの喪失)、α2↑(大分子量蛋白：ハプトグロビン、α2-マクログロブリン)
- 肝硬変：(Alb、α1、α2)↓(蛋白産生低下)、γ↑、β-γ bridging(トランスフェリン減少、γグロブリン増加)
- 多発性骨髄腫、マクログロブリン血症、良性M蛋白血症など：α2-γに急峻なピーク(M蛋白のピーク)
「fractionation」
- n.
- 関
- cleavage、cleave、contingency、divide、division、fraction、fractional、fractionate、mince、parcellated、part、parted、partition、resolution、split