• Title/Summary/Keyword: Protein-1

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A Study of the Foaming Poperties of Mungbean Protein Isolate (녹두 단백질의 기포특성에 관한 연구)

  • 민성희;손경희
    • Korean journal of food and cookery science
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    • v.4 no.2
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    • pp.1-9
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    • 1988
  • This study was carried out in order to study the foaming properties of mungbean protein. Mungbean protein isolate was tested for the purpose of finding out the effect of pH, addition of sucrose on foaming properties. The results were summarized as follows: 1. Foam expansion values were generally depen. dent on protein concentration to 3% protein suspension. From 1% to 3% suspension, foam expansion values increased. However over 3% suspension, the values decreased. In 1% mungbean protein suspension, the foam expansion value of suspension at pH 4.5 was greater than that of at pH9. In 3%, 5%, and 10% suspensiona the foam expansion values of suspension at pH 7 was the lowest. Foam expansion value significantly decreased by the addition of sucrose. 2. The foam stability appeared the greatest value as protein concentration increased. It appeared the greatest value at pH 4.5. When sucrose was added, the foam stability increased. The more sucrose was added, the better foam stability was.

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Probing α/β Balances in Modified Amber Force Fields from a Molecular Dynamics Study on a ββα Model Protein (1FSD)

  • Yang, Changwon;Kim, Eunae;Pak, Youngshang
    • Bulletin of the Korean Chemical Society
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    • v.35 no.6
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    • pp.1713-1719
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    • 2014
  • 1FSD is a 28-residue designed protein with a ${\beta}{\beta}{\alpha}$ motif. Since this protein displays most essential features of protein structures in such a small size, this model protein can be an outstanding system for evaluating the balance in the propensity of the secondary structures and the quality of all-atom protein force fields. Particularly, this protein would be difficult to fold to its correct native structure without establishing proper balances between the secondary structure elements in all-atom energy functions. In this work, a series of the recently optimized five amber protein force fields [$ff03^*$, $f99sb^*$-ildn, ff99sb-${\phi}^{\prime}$-ildn, ff99sb-nmr1-ildn, ff99sb-${\Phi}{\Psi}$(G24, CS)-ildn] were investigated for the simulations of 1FSD using a conventional molecular dynamics (MD) and a biased-exchange meta-dynamics (BEMD) methods. Among those tested force fields, we found that ff99sb-nmr1-ildn and ff99sb-${\Phi}{\Psi}$(G24, CS)-ildn are promising in that both force fields can locate the native state of 1FSD with a high accuracy (backbone rmsd ${\leq}1.7{\AA}$) in the global free energy minimum basin with a reasonable energetics conforming to a previous circular dichroism (CD) experiment. Furthermore, both force fields led to a common set of two distinct folding pathways with a heterogeneous nature of the transition state to the folding. We anticipate that these force fields are reasonably well balanced, thereby transferable to many other protein folds.

Separation and Composition of Sesame Meal Protein (참깨박(粕) 단백질(蛋白質)의 분리(分離)와 조성(組成))

  • Kim, Jun-Pyong;Shim, Woo-Man;Kim, Chong-Ik
    • Applied Biological Chemistry
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    • v.23 no.1
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    • pp.14-22
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    • 1980
  • White and black sesame produced in Korea were defatted with ethyl ether or n-hexane. Defatted sesame meal was extracted with water and salt solution, and protein extraction was precipitated at various pH 1 through 12, with trichloro acetic acid (TCA), tannic acid and ammonium sulfate, respectively. Protein was purified by Sephadex A-25, G-75, G-100 and G-200, and identified its protein fraction by polyacrylamide gel electrophoresis. Amino acids composition of protein in white sesame was analyzed by automatic amino acid analyzer. Protein contents of white sesame, black sesame and sesame meal are 20.5%, 19.2%, and 44.7%, respectively. n-Hexane was the most suitable solvent for extraction of oil from sesame. Crude protein precipitation was better in higher pH. The protein extraction was more effective with the solution containing sodium chloride tinder the pH 8. Globulin in total protein was high and prolamin was less than in other cereal proteins. Glutamic acid contents of white sesame and sesame globulin were 17.1%, and 20%, respectively. Both proteins contained relatively high levels of essential amino acids. 12-13 bands were found in water soluble protein and 2 bands in salt soluble protein were detected by the disc gel electrophoresis, and were identified in both of white and black sesame. The salt soluble protein of white sesame could be purified by Sephadee G-100 and G-200.

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Effect of Non- Protein Nitrogen on the Biological Utilization of Protein and the Excretion of Nitrogenous Compounds in Chicks (병아리에서 단백질의 생물적 이용성과 요중질소 화합물의 배설에 미치는 비단백태질소의 영향)

  • 고태송;김영범;서인준;남기택
    • Korean Journal of Poultry Science
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    • v.12 no.1
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    • pp.17-24
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    • 1985
  • In order to investigate an effect of non-protein nitrogen on the biological utilization of protein, hatched single comb White Leghorn male chicks were fed for the first 8 days with a commercial chicks mash, next 6 days with protein-free diet and subsequent 6 days with protein-free diets and protein diets containing 10.59% of crude protein supplemented with 0, 0.5, 1.0 and 1.5%, respectively. During experimental feeding period, chicks fed protein-free diets had intaked gradually lower feed and had shown a similar body weight loss though urea contents were increased. When birds fed protein diets, body weight gain and feed intake were not different among birds fed the graded levels of urea although feed conversions were shown a highering tendency along with increasing urea contents. According as supplemented urea were increased, protein efficiency ratio f (PER) and net protein ratio (NPR) were increased in chicks fed protein-free diets, which were shown a lowering trend in chicks fed protein diets. Effect of supplemented urea on the urinary excretion of uric acid were not found in birds fed protein-free diets, while which were increased in birds fed protein diets with the increase of urea contents. Urea addition did not affect the excretion of total creatine in birds fed protein-free or protein diets. Excretion of ammonia was jogjered in order to increasing level of urea in birds fed protein-free diets, but which were not found any particular effect in birds fed protein diets. Also urea excretion were gradually increased with the increasing contents of urea in protein-free and protein diets. Nitrogen balance of birds fed protein-free diets were minus values, which were increased with increasing urea contents in diets. When birds fed protein diets, nitrogen balance and urinary nitrogen excretion was highered and fecal nitrogen excretion were not altered as urea levels of diets increased. Digestibility of urea nitrogen supplemented in protein-free diets were lowered along with increasing contents of urea, but biological value(BV) and net protein utilization(NPU) was found a highering tendency in birds fed protein-free diet containing 1.5% of urea. When birds fed with protein diets, digestibility, BV and NPU of protein were found a highering trend in birds fed protein diets added with 0.5% of urea.

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Human Ribosomal Protein L18a Interacts with hnRNP E1

  • Han, Sun-Young;Choi, Mie-Young
    • Animal cells and systems
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    • v.12 no.3
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    • pp.143-148
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    • 2008
  • Heterogeneous nuclear ribonucleoprotein E1(hnRNP E1) is one of the primary pre-mRNA binding proteins in human cells. It consists of 356 amino acid residues and harbors three hnRNP K homology(KH) domains that mediate RNA-binding. The hnRNP E1 protein was shown to play important roles in mRNA stabilization and translational control. In order to enhance our understanding of the cellular functions of hnRNP E1, we searched for interacting proteins through a yeast two-hybrid screening while using HeLa cDNA library as target. One of the cDNA clones was found to be human ribosomal protein L18a cDNA(GenBank accession number BC071920). We demonstrated in this study that human ribosomal protein L18a, a constituent of ribosomal protein large subunit, interacts specifically with hnRNP E1 in the yeast two-hybrid system. Such an interaction was observed for the first time in this study, and was also verified by biochemical assay.

Changes in in vivo ruminal fermentation patterns and blood metabolites by different protein fraction-enriched feeds in Holstein steers

  • Choi, Chang Weon
    • Korean Journal of Agricultural Science
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    • v.44 no.3
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    • pp.392-399
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    • 2017
  • The present study was conducted to investigate the effects of different dietary proteins as fraction-enriched protein, defined by Cornell net carbohydrates and protein system (CNCPS), on in vivo ruminal fermentation pattern and blood metabolites in Holstein steers fed total mixed ration (TMR) containing 17.2% crude protein. Four ruminally cannulated Holstein steers in a $4{\times}4$ Latin square design consumed TMR only (control) and TMR with rapeseed meal (AB1), soybean meal (B2), and perilla meal (B3C). Each protein was substituted for 23.0% of crude protein in TMR. Rumen digesta were taken through ruminal cannula at 1 h interval during the feeding cycle in order to analyze ruminal pH, ammonia-N, and volatile fatty acids (VFA). Plasma metabolites in blood taken via the jugular vein after the rumen digesta sampling were analyzed. Feeding perilla meal significantly (p < 0.05) decreased mean ruminal pH compared with control and the other protein feeding groups. Compared with control, feeding protein significantly (p < 0.05) increased ruminal ammonia-N concentration except for AB1. Statistically (p > 0.05) similar total VFA appeared among control and the supplemented groups. However, control, AB1, and B2 showed higher (p < 0.05) acetate concentrations than B3C, and propionate was vice versa. CNCPS fractionated protein significantly (p < 0.05) affected concentrations of albumin and total protein in blood; i.e. plasma albumin was lower for control and B2 groups than AB1 and B3C groups. Despite lack of significances (p > 0.05) in creatinine and blood urea nitrogen, AB1 and B2 groups were numerically higher than the others.

Inheritance of Cgy1 gene and Ti gene in Mature Soybean Seed

  • Sung, Mi-Kyung;Han, Eun-Hui;Kim, Kyung-Roc;Park, Jung-Soo;Hwang, Kyo-Jin;Nam, Jin-Woo;Chung, Jong-Il
    • Korean Journal of Breeding Science
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    • v.42 no.1
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    • pp.35-39
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    • 2010
  • Soybean proteins are widely used for human and animal feed in the world. ${\beta}$-conglycinin protein exhibits poor nutritional and food processing properties and Kunitz trypsin inhibitor (KTI) protein is a main anti-nutritional factor in soybean seed. The objective of this research was to identify the inheritance of $cgy_1$ gene and ti gene for the improvement of soybean cultivar with no KTI proteins and low amount of ${\beta}$-conglycinin. $F_2$ population was made by crossing between "Gaechuck2ho" (${\alpha}^{\prime}$-subunit present $Cgy_1Cgy_1$, KTI protein absent titi) and PI506876 (${\alpha}^{\prime}$-subunit absent $cgy_1cgy_1$, KTI protein present TiTi) parent. A total of 434 $F_2$ seeds were obtained and analyzed for the segregation of ${\alpha}^{\prime}$-subunit protein and KTI protein using SDS-PAGE. The segregation ratio of 3 : 1 for $Cgy_1$ locus (310 $Cgy_1$_ : 124 $cgy_1cgy_1$) and Ti locus (339 Ti_ : 95 titi) were observed. Segregation ratios of 9 : 3 : 3 : 1 (241 $Cgy_1$_Ti_: 69 $Cgy_1$_titi: 98 $cgy_1cgy_1$Ti_: 26 $cgy_1cgy_1titi$) between $Cgy_1$ gene and Ti gene in $F_2$ seeds were also observed (${\chi}^2= 5.367$, P = 0.10 - 0.20). This data showed that $Cgy_1$ gene was inherited independently with the Ti gene in soybean. These results will be useful in breeding program for selecting the line that does not exhibit or lacks both ${\alpha}^{\prime}$-subunit protein and KTI protein in soybean.

The Bacteriophage λ DNA Replication Protein P Inhibits the oriC DNA- and ATP-binding Functions of the DNA Replication Initiator Protein DnaA of Escherichia coli

  • Datta, Indrani;Sau, Subrata;Sil, Alok Kumar;Mandal, Mitai C.
    • BMB Reports
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    • v.38 no.1
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    • pp.97-103
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    • 2005
  • Under the condition of expression of $\lambda$ P protein at lethal level, the oriC DNA-binding activity is significantly affected in wild-type E. coli but not in the rpl mutant. In purified system, the $\lambda$ P protein inhibits the binding of both oriC DNA and ATP to the wild-type DnaA protein but not to the rpl DnaA protein. We conclude that the $\lambda$ P protein inhibits the binding of oriC DNA and ATP to the wild-type DnaA protein, which causes the inhibition of host DNA synthesis initiation that ultimately leads to bacterial death. A possible beneficial effect of this interaction of $\lambda$ P protein with E. coli DNA initiator protein DnaA for phage DNA replication has been proposed.

Phosphorylation of $Ser^{246}$ Residue in Integrin-linked Kinase 1 by Serum- and Glucocorticoid-induced Kinase 1 is Required to Form a Protein-protein Complex with 14-3-3

  • Chun, Jae-Sun;Kang, Sang-Sun
    • Animal cells and systems
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    • v.9 no.3
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    • pp.161-171
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    • 2005
  • Integrin-linked kinase 1 (ILK1) regulates several protein kinases, including PKB/Akt kinase and glycogen synthase kinase ${\beta}$. ILK1 is also involved distinctively in the cell morphological and structural functions by interacting with the components of the extracellular matrix or integrin. According to the information of serum- and glucocorticoid-induced kinase 1 (SGK1) substrate specificity (R-X-R-X-X(S/T)-${\phi};{\phi}$ indicates a hydrophobic amino acid), two putative phosphorylation sites, $Thr^{181}\;and\;Ser^{246}$, were found in ILK1. We showed that ILK1 fusion protein and two fluorescein-labeled ILK1 peptides, $FITC-^{174}RTRPRNGTLN^{183}$ and $FITC-^{239}CPRLRIFSHP^{248}$, were phosphorylated by SGK1 in vitro. We also identified that 14-3-3 ${\theta}\;{\varepsilon}\;and\;{\xi}$, among several 143-3 isotypes $({\beta},\;{\gamma},\;{\varepsilon},\;{\eta},\;{\sigma},\;{\theta},\;{\tau}\;and\;{\xi})$ formed protein complex with ILK1 in COS-1 cells. Furthermore, the phosphorylation of $Ser^{246}$ by SGK1 induced the binding with 14-3-3. It was also demonstrated that 14-3-3-bound ILK1 has reduced kinase activity. Thus, these data suggest that SGK1 phosphorylates $Thr^{181}\;and\;Ser^{246}$ of ILK1 and the phosphorylation of its $Ser^{246}$ makes ILK1 bind to 14-3-3, resulting in the inhibition of ILK1 kinase activity.

Transcriptomic analysis of 'Campbell Early' and 'Muscat Bailey A' grapevine shoots exposed to freezing cold stress (영하의 저온에 노출된 'Campbell Early'와 'Muscat Bailey A' 포도나무 신초의 전사체 비교)

  • Kim, Seon Ae;Yun, Hae Keun
    • Journal of Plant Biotechnology
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    • v.43 no.2
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    • pp.204-212
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    • 2016
  • To understand the responses of grapevines in response to cold stress causing the limited growth and development, differentially expressed genes (DEGs) were screened through transcriptome analysis of shoots from 2 grapevine cultivars ('Campbell Early' and 'Muscat Baily A') kept at -$2^{\circ}C$ for 4 days. In gene ontology analysis of DEGs from 'Campbell Early', there were 17,424 clones related with biological process, 28,954 with cellular component, and 6,972 with molecular function genes in response to freezing temperature. The major induced genes included dehydrin xero 1, K-box region and MADS-box transcription factor family protein, and MYB domain protein 36, and inhibited genes included light-harvesting chlorophyll B-binding protein 3, FASCICLIN-like arabinoogalactan 9, and pectin methylesterase 61 in 'Campbell Early' grapevines. In gene ontology analysis of DEGs from 'Muscat Baily A', there were 1,157 clones related with biological process, 1,350 with cellular component, and 431 with molecular function gene. The major induced genes of 'Muscat Baily A' included NB-ARC domain-containing disease resistance protein, fatty acid hydrozylase superfamily, and isopentenyltransferase 3, and inhibited genes included binding, IAP-like protein 1, and pentatricopeptide repeat superfamily protein. All major DEGs were shown to be expressed differentially by freezing temperature in real time-PCR analysis. Protein domain analysis using InterPro Scan revealed that ubiquitin-protein ligase was redundant in both tested grapevines. Transcriptome profile of shoots exposed to cold can provide new insights into the molecular basis of tolerance to low-temperature in grapevines, and can be used as resources for development new grapevines tolerant to coldness.