• Title/Summary/Keyword: Protein C

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A Conserved Structure and Function of the YidC Homologous Protein Slr1471 from Synechocystis sp. PCC 6803

  • GathmannI, Sven;Rupprecht, Eva;Kahmann, Uwe;Schneider, Dirk
    • Journal of Microbiology and Biotechnology
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    • v.18 no.6
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    • pp.1090-1094
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    • 2008
  • In this article, we show that the orf slr1471 from Synechocystis sp. PCC 6803 codes for a functional member of the YidC/Alb3/Oxa1 protein family, and the encoded protein has a transmembrane topology with a common core structure. Using specific antibodies raised against the Synechocystis YidC homologous protein, we further show that the Synechocystis YidC protein appears to be predominantly localized in the cyanobacterial cytoplasmic membrane. The impact of the described findings for synthesis of membrane proteins and for protein sorting within cyanobacterial cells is discussed.

Effect of Dietary Protein and Lipid Levels on Compensatory Growth of Juvenile Olive Flounder (Paralichthys olivaceus) Reared in Suboptimal Temperature

  • Cho, S.H.
    • Asian-Australasian Journal of Animal Sciences
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    • v.24 no.3
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    • pp.407-413
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    • 2011
  • Effect of dietary protein and lipid levels on compensatory growth of juvenile olive flounder (Paralichthys olivaceus) was determined in suboptimal temperature ($13.4{\pm}1.42^{\circ}C$). Five hundred forty fish averaging 79.2 g were randomly distributed into 27 of 300 L flow-through tanks (20 fish/tank). Nine treatments were prepared in triplicate: fish were hand-fed with control (C) diet for 10 weeks (10WF-C); four fish groups were starved for 1 week and then fed with C, high protein (HP), high lipid (HL) and combined high protein and high lipid (HPL) diets for 9 weeks, referred to as 9WF-C, 9WF-HP, 9WF-HL, 9WF-HPL, respectively; and other four fish groups were starved for 2 weeks and then fed with C, HP, HL and HPL diets for 8 weeks, referred to as 8WF-C, 8WF-HP, 8WF-HL and 8WF-HPL, respectively. Weight gain and specific growth rate of fish in 9WF-HP, 9WF-HPL, 8WF-HP and 8WF-HPL treatments were higher than those of fish in 9WF-HL and 8WF-HL treatments. Feed efficiency of fish in 8WF-HP treatment was higher than that of fish in 9WF-C, 9WF-HL and 8WF-HL treatments. Protein efficiency ratio of fish in 10WF-C, 8WF-C, 8WF-HP and 8WF-HPL treatments was higher that that of fish in 9WF-HL and 8WF-HL treatments. Juvenile olive flounder subjected to 2-week feed deprivation could achieve full compensatory growth with dietary supplementation of protein or combined high protein and high lipid.

Protein Kinase A Increases DNA-Binding Activity of Testis-Brain RNA-Binding Protein

  • Ju, Hyun-Hee;Ghil, Sung-Ho
    • Biomedical Science Letters
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    • v.14 no.2
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    • pp.77-81
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    • 2008
  • Testis brain RNA-binding protein (TB-RBP) is a DNA/RNA binding protein. TB-RBP is mainly expressed in testis and brain and highly conserved protein with several functions, including chromosomal translocations, DNA repair, mitotic cell division, and mRNA transport, stabilization, and storage. In our previous study, we identified TB-RBP as an interacting partner for the catalytic subunit $(C{\alpha})$ of protein kinase A(PKA) and verified their interaction with several biochemical analyses. Here, we confirmed interaction between $C{\alpha}$. and TB-RBP in mammalian cells and determined the effect of $C{\alpha}$. on the function of TB-RBP. The activation of $C{\alpha}$. increased the TB-RBP function as a DNA-binding protein. These results suggest that the function of TB-RBP can be modulated by PKA and provide insights into the diverse role of PKA.

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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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    • v.12 no.6
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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.

Protein Production from Cellulosic Wastes by Mixed Culture of A. phoenices and C. utilis (Aspergillus phoenicis 및 candida utilis의 혼합배양에 의한 섬유소로부터의 단백질 생산)

  • 이영녹;박경량;이주실;배광성;백대홍
    • Korean Journal of Microbiology
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    • v.19 no.1
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    • pp.14-22
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    • 1981
  • Protein content of cellulosic wastes, such as spent grain, hop bark, spent rye, rice straw, rice hull, saw dust and used newspaper, was increased by a mixed culture of C. utilis wastes having 66-75% moisture. Among the fungal strains tested. A.phoenicis KU175 was the most powerful to increase the protein content of A. phoenicis during the mixed culture with C. utilis in the CMC medium reached at the peak for one day culture after inoculation of the both strains at the same time, while it reached at peark from the beginning of the mixed culture, when A. phoenicis was inocultated for 12-24hours prior to the inoculation of C.utilis. To increase the protein content of the cellulosic wastes by the mixed culture of C.utilis and A.phoenicis, the inoculation of both strains at the same time was more effective than the preinoculation of A. phoenicis for 6-24 hours. Content of crude cellulose in the used newspaper, saw dust and spent grain was high relatively, and the lignin content of spent grain, spent rye, and rice strew was reduced more than half by the treatment of 2% NaOH. However, effect of alkali treatment of increase the protein content of the cellulosic wastes was not prominent in the case of mixed culture. Protein content of the cellulosic wastes was increased prominently by the mixed culture of C.utilis and A.phoenicis in semi-solid substrate, compared with the single culture of C. utilis, although the latter increased the protein content of cellulosic wastes considerably. The effect of mixed culture of C. utilis and A. phoenicis increased 4-fold the protein content of spent grain, and more than doubled crude protein in hop bark and rice straw.

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Effect of Vitamin C, Silicon and Iron on Collagen Synthesis and Break-Down Enzyme Expression in the Human Dermal Fibroblast Cell (HS27) (피부 섬유아세포에서 비타민 C, Silicon, 철분 처리가 콜라겐 합성 및 분해 관련 효소의 발현에 미치는 효과 비교)

  • Kim, Jeong-Eun;Lee, Jin-Ah;Kim, Hyun-Ae;Kim, Jung-Min;Cho, Yun-Hi
    • Journal of Nutrition and Health
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    • v.42 no.6
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    • pp.505-515
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    • 2009
  • Collagen is the major matrix protein in dermis and consists of proline and lysine, which are hydroxylated by prolyl hydroxylase (PH) and lysyl hydroxylase (LH) with cofactors such as vitamin C, oxygen, iron (Fe$^{2+}$), ketoglutarate and silicon. The collagen degradation is regulated by matrix metalloproteinase-1 (MMP-1), of which is the major collagen-degrading proteinase whereas tissue inhibitors of metalloproteinase-1 (TIMP-1) bind to MMP-1 thereby inhibiting MMP-1 activity. In this study, we investigated the effects of vitamin C, silicon and iron on mRNA, protein expressions of PH, LH, MMP-1 and TIMP-1. The physiological concentrations of vitamin C (0-100 $\mu$M), silicon (0-50 $\mu$M) and iron (Fe$^{2+}$:0-50 $\mu$M) were treated to human dermal fibroblast cells (HS27 cells) for 3 or 5days. The expression level of mRNA and protein was increased in not only PH but also LH when cells were incubated with vitamin C. A similar increase in LH mRNA or protein expression occurred when cells were incubated with silicon. Our results suggest that treatment of vitamin C and silicon increased mRNA and protein expression of PH and LH in human dermal fibroblast.

A LIM Protein Gene Homologue of Protaetia brevitarsis: cDNA Cloning and mRNA Expression

  • Kim Iksoo;Choi Yong Soo;Lee Sun Young;Kim Mi Ae;Kim Seong Ryul;Hwang Jae Sam;Jin Byung Rae
    • International Journal of Industrial Entomology and Biomaterials
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    • v.11 no.1
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    • pp.71-74
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    • 2005
  • A LIM protein gene homologue of the CRP (cysteine­rich protein) family in the whiter-spotted flower chafer, Protaetia brevitarsis, was cloned. The P. brevitarsis LIM protein cDNA encodes a 92 amino acid polypep­tide with a predicted molecular mass of 10,030 Da and a pI of 8.57. The P. brevitarsis LIM protein contains the cysteine-rich consensus sequence of LIM domain and the glycine-rich consensus sequence observed in the cysteine-rich protein family 1 (CRPl). The potential nuclear targeting signal is retained. The deduced amino acid sequence of the P. brevitarsis LIM protein cDNA showed 92$\%$ identity to another beetle, Apriona germari LIM protein. Northern blot analysis showed that P. brevitarsis LIM protein is highly expressed in epidermis and midgut, but not in the fat body.

Molecular Cloning and Expression of a cDNA Encoding Putative Chemosensory Protein from the Mole Cricket, Gryllotalpa orientalis

  • Kim, Iksoo;Lee, Kwang-Sik;Ryu, Kang-Sun;Kim, Jin-Woo;Ahn, Mi-Young;Lee, Heui-Sam;Sohn, Hung-Dea;Jin, Byung-Rae
    • International Journal of Industrial Entomology and Biomaterials
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    • v.6 no.1
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    • pp.87-92
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    • 2003
  • We describe here the cloning, expression and characterization of a cDNA encoding a putative chemosensory protein (CSP) from the mole cricket, Gryllotalpa orientalis. The G. orientalis chemosensory protein cDNA sequences comprised of 384 bp with 128 amino acid residues. The G. orientalis chemosensory protein showed 75.4% protein sequence identity to the Locusta migratoria CSP, Northern blot analysis revealed that signal was stronger in head than leg and cuticle, indicating that the head part containing antennae is a main site for G. orientalis chemosensory protein synthesis. The cDNA encoding G. orientalis chemosensory protein was expressed as approximately 12 kDa polypeptide in baculovirus-infected insect cells.

Effects of Heating Time and Temperature on Functional Properties of Proteins of Yellow Mealworm Larvae (Tenebrio molitor L.)

  • Lee, Ha-Jung;Kim, Ji-Han;Ji, Da-Som;Lee, Chi-Ho
    • Food Science of Animal Resources
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    • v.39 no.2
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    • pp.296-308
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    • 2019
  • Although the yellow mealworm (Tenebrio molitor L.) is a promising alternative protein source, the effects of processing conditions on functional properties are unclear. In this study, a protein extract of yellow mealworm larvae (PEYM) was subjected to different heat temperature ($55^{\circ}C$, $75^{\circ}C$, and $95^{\circ}C$) with different time (20, 40, and 60 min) to evaluate the functional properties and protein oxidation. Different heat temperature treatment significantly affected the exposure of surface hydrophobicity of the proteins and protein molecule aggregation, which reached maximum levels at $95^{\circ}C$ for 60 min. Protein oxidation was inversely proportional to the temperature. Both the highest carbonyl value (1.49 nmol/mg protein) and lowest thiol value (22.94 nmol/mg protein) were observed at $95^{\circ}C$ for 60 min. The heating time-temperature interaction affected several functional properties, including solubility, emulsifying potential, and gel strength (GS). Solubility decreased near the isoelectric point (pH 5 to 6). As the temperature and heating time increased, emulsifying properties decreased and GS increased. The oil absorption capacity and foaming properties decreased and the water absorption capacity increased. These results confirmed that PEYM is a suitable source of proteins for processing and applications in the food industry.

Phosphorylation of Transcriptional Factor by Mitogen-activated Protein (MAP) Kinase Purified from Nucleus (핵 내에서 분리한 Mitogen-Activated Protein (MAP) Kinase의 Transcription Factor에 대한 인산화)

  • 김윤석;김소영;김태우
    • Biomedical Science Letters
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    • v.2 no.2
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    • pp.175-185
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    • 1996
  • The mitogen-activated protein(MAP) kinase signal transduction pathway represents an important mechanism by which mitogen, such as serum and PMA, regulate cell proliferation and differentiation. Target substrates of the MAP kinase are located within several compartments containing plasma membranes and nucleus. We now report that serum addition induces proliferation of the P388 murine leukemia cell, but PMA does not, while both serum and PMA treatment cause translocation of the MAP kinase, mainly p42$^{mapk}$ isoform, from cytosol into the nucleus, which was monitored by immunoblot analysis using polyclonal anti-ERK1 antibodies. We investigated whether the MAP kinase was capable of phosphorylating c-Jun protein and GST-fusion proteins, the P562$^{kk}$N-terminal peptides (1-77 or 1-123 domain) of the T cell tyrosine kinase, using the partially purified MAP kinase by SP-sephadex C-50, phenyl superose and Mono Q column chromatography. We found that the partially purified MAP kinase was able to phosphorylate c-Jun protein and the GST-fusion protein expressed using E.coli DH5$\alpha$ which is transformed with pGEX-3Xb plasmid vector carrying of p562$^{kk}$N-terminal peptide-encoding DNA. These results imply that tyrosine kinase receptor/Ras/Raf/MAP kinase pathway is a major mechanism for mitogen-induced cell proliferation in P388 murine leukemia cell and that the various MAP kinase isoforms may have their own target substrates located in distinct subcellular compartments.

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