• Title/Summary/Keyword: C5 Protein

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Influence of Yeast Fermented Cassava Chip Protein (YEFECAP) and Roughage to Concentrate Ratio on Ruminal Fermentation and Microorganisms Using In vitro Gas Production Technique

  • Polyorach, S.;Wanapat, M.;Cherdthong, A.
    • Asian-Australasian Journal of Animal Sciences
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    • v.27 no.1
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    • pp.36-45
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    • 2014
  • The objective of this study was to determine the effects of protein sources and roughage (R) to concentrate (C) ratio on in vitro fermentation parameters using a gas production technique. The experimental design was a $2{\times}5$ factorial arrangement in a completely randomized design (CRD). Factor A was 2 levels of protein sources yeast fermented cassava chip protein (YEFECAP) and soybean meal (SBM) and factor B was 5 levels of roughage to concentrate (R:C) ratio at 80:20, 60:40, 40:60, 20:80, and 0:100, respectively. Rice straw was used as a roughage source. It was found that gas production from the insoluble fraction (b) of YEFECAP supplemented group was significantly higher (p<0.05) than those in SBM supplemented group. Moreover, the intercept value (a), gas production from the insoluble fraction (b), gas production rate constants for the insoluble fraction (c), potential extent of gas production (a+b) and cumulative gas production at 96 h were influenced (p<0.01) by R:C ratio. In addition, protein source had no effect (p>0.05) on ether in vitro digestibility of dry matter (IVDMD) and organic (IVOMD) while R:C ratio affected the IVDMD and IVOMD (p<0.01). Moreover, YEFECAP supplanted group showed a significantly increased (p<0.05) total VFA and $C_3$ while $C_2$, $C_2:C_3$ and $CH_4$ production were decreased when compared with SBM supplemented group. In addition, a decreasing R:C ratio had a significant effect (p<0.05) on increasing total VFA, $C_3$ and $NH_3$-N, but decreasing the $C_2$, $C_2:C_3$ and CH4 production (p<0.01). Furthermore, total bacteria, Fibrobacter succinogenes, Ruminococcus flavefaciens and Ruminococcus albus populations in YEFECAP supplemented group were significantly higher (p<0.05) than those in the SBM supplemented group while fungal zoospores, methanogens and protozoal population remained unchanged (p>0.05) as compared between the two sources of protein. Moreover, fungal zoospores and total bacteria population were significantly increased (p<0.01) while, F. succinogenes, R. flavefaciens, R. albus, methanogens and protozoal population were decreased (p<0.01) with decreasing R:C ratio. In conclusion, YEFECAP has a potential for use as a protein source for improving rumen fermentation efficiency in ruminants.

Effects of Staurosporine and Genistein on Superoxide Generation and Degranulation in PMA- or C5a-Activated Neutrophils

  • Ha, Sung-Heon;Lee, Chung-Soo
    • BMB Reports
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    • v.28 no.3
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    • pp.210-215
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    • 1995
  • Effects of staurosporine, genistein and pertussis toxin on PMA-induced superoxide generation and degranulation in neutrophils were investigated. Their effects were also examined in C5a-stimulated superoxide generation. PMA-induced superoxide generation was inhibited by staurosporine but was not affected by pertussis toxin. Genistein enhanced the stimulatory effect of PMA in a dose dependent fashion. C5a-induced superoxide generation was inhibited by staurosporine, genistein and pertussis toxin. An NADPH oxidase system of resting neutrophils was activated by PMA, and the stimulatory effect of PMA was inhibited by staurosporine but was not affected genistein and pertussis toxin. The activity of NADPH oxidase in the membrane fraction of PMA-activated neutrophils was not affected by staurosporine and genistein. PMA-induced acid phosphatase release was inhibited by staurosporine and genistein, whereas the effect of pertussis toxin was not detected. These results suggest' that the role of protein tyrosine kinase in neutrophil activation mediated by direct activation of protein kinase C may be different from receptor-mediated activation. The action of protein kinase C on the respiratory burst might be affected by the change of protein tyrosine kinase activity.

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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.

Cold Adaptation of Lactobacillus paraplantarum C7 Isolated from Kimchi

  • Kim, Su-Jung;Kim, Jong-Hwan;Park, Jae-Yong;Kim, Han-Taek;Jeong, Seon-Ju;Ha, Yeong-Lae;Yun, Han-Dae;Kim, Jeong-Hwan
    • Journal of Microbiology and Biotechnology
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    • v.14 no.5
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    • pp.1071-1074
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    • 2004
  • The effect of preadaptation at low temperature on cryoprotection was studied for Lactobacillus paraplantarum C7, a bacteriocin producer isolated from kimchi. L paraplantarum C7 cells in their log growth phase were incubated at $15^\circ{C}$, $10^\circ{C}$, or $5^\circ{C}$ for 2, 4, and 6 h, respectively, before being frozen at $-70^\circ{C}$. After 24 h of freezing, viable cells were counted after brief thawing. The freezing-thawing cycles were repeated three more times. Cells preadapted at $10^\circ{C}$ or $5^\circ{C}$ before freezing survived better than control cells, but preadaptation at $15^\circ{C}$ did not confer cryoprotection. Chloramphenicol addition did not destroy the cryoprotection, indicating that protein synthesis was not required for the development of cryoprotection. SDS-PAGE showed induction of a 6.5-kDa protein, a major cold-shock protein, in preadapted cells.

The C-terminal Region of Human Tau Protein with Ability of Filament Formation

  • Chung, Sang-Ho
    • Animal cells and systems
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    • v.1 no.2
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    • pp.317-321
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    • 1997
  • Tau protein is one of the microtubule-associated proteins in the mammalian brain. In Alzheimer's disease, tau protein is immobilized in the somatodendritic compartment of certain nerve cells, where it forms a part of the paired helical filament (PHF). To understand the role of tau protein in the formation of PHF, a recombinant human tau protein expressed in Escherichia coli and five synthetic peptide fragments (peptide 1 to peptide 5), corresponding to the C-terminal region of tau protein, were prepared and their ability in self-assembly to form filamentous structures was examined. The recombinant human tau protein formed short rod-like structures in 0.1M MES buffer containing 1 mM $MgCI_2$, while a synthetic peptide fragment 1 containing 55 amino acid residues could assemble into a lot of long filamentous structures in water and particularly twisted helical structures in 0.1M MES buffer containing 1 mM $MgCI_2$. This suggests that the C-terminal region possesses a filament-forming ability and may be related to the formation of the helical structure by providing a powerful filament-forming driving force.

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Backbone 1H, 15N, and 13C Resonance Assignments and Secondary-Structure of Conserved Hypothetical Protein HP0894 from Helicobacter pylori

  • Han, Kyung-Doo;Park, Sung-Jean;Lee, Bong-Jin
    • Molecules and Cells
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    • v.20 no.3
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    • pp.442-445
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    • 2005
  • HP0894 (SwissProt/TrEMBL ID O25554) is an 88-residue conserved hypothetical protein from Helicobacter pylori strain 26695 with a calculated pI of 8.5 and a molecular weight of 10.38 kDa. Proteins with sequence similarity to HP0894 exist in Vibrio choierae, Enterococcus faecalis, Campylobacter jejuni, Streptococcus pneumoniae, Haemophilus influenzae, Escherichia coli O157, etc. Here we report the sequence-specific backbone resonance assignments of HP0894. About 97.5% (418/429) of the HN, N, CO, $C{\alpha}$, $C{\beta}$ resonances of the 88 residues of HP0894 were assigned. On the basis of these assignments, three helical regions and four strand regions were identified using the CSI program. This study is a prerequisite for calculating the solution structure of HP0894, and studying its interaction with its substrates, if any, and/or with other proteins.

Cyclodextrin Glucanotransferase from Bacillus stearothermophilus:Purification by Affinity Chromatography and Its Properties (Bacillus stearothermophilus가 생산하는 Cyclodextrin Glucanotransferase: Affinity Chromatography를 이용한 정제 및 성질)

  • 안중훈;황진봉;김승호
    • Microbiology and Biotechnology Letters
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    • v.18 no.6
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    • pp.585-590
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    • 1990
  • The cyclodextrin glucanotransferase (CGTase) was purified from the culture broth of Bacillus stearothermophilus by ammonium sulfate precipitation and affinity chromatography. The specific activity of the CGTase increased by about 31-fold from 111.5 U/mg protein to 3445.0 Ulmg protein. The SDSPAGE indicated that the purified CGTase was homogeneous and the molecular weight of the purified CGTase was about 78,000. The optimum pH and temperature was 6.0 and $60^{\circ}C$, respectively. This enzyme was stable from pH 5.5-10.0. The enzyme retained its full activity at the incubation temperature up to $60^{\circ}C$ and calcium ion increased the thermal stability. The isoelectric point was about 4.8.

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The effect of eleutherococcus senticosus on metabolism-associated protein expression in 3T3-L1 and C2C12 cells

  • Hashimoto, Takeshi;Okada, Yoko;Yamanaka, Atsushi;Ono, Natsuhiko;Uryu, Keisuke;Maru, Isafumi
    • Korean Journal of Exercise Nutrition
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    • v.24 no.3
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    • pp.13-18
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    • 2020
  • [Purpose] In vivo studies have demonstrated the ergogenic benefits of eleutherococcus senticosus (ES) supplementation. ES has been observed to enhance endurance capacity, improve cardiovascular function, and alter metabolic functions (e.g., increased fat utilization); however, the exact mechanisms involved remain unknown. We aimed to determine whether ES could effectively induce fat loss and improve muscle metabolic profiles through increases in lipolysis- and lipid metabolism-associated protein expression in 3T3-L1 adipocytes and C2C12 skeletal muscle cells, respectively, to uncover the direct effects of ES on adipocytes and skeletal muscle cells. [Methods] Different doses of ES extracts (0.2, 0.5, and 1.0 mg/mL) were added to cells (0.2 ES, 0.5 ES, and 1.0 ES, respectively) for 72 h and compared to the vehicle control (control). [Results] The intracellular triacylglycerol (TG) content significantly decreased (p < 0.05 for 0.2 ES, p < 0.01 for 0.5 ES and 1.0 ES) in 3T3-L1 cells. Adipose triglyceride lipase, which is involved in active lipolysis, was significantly higher in the 1.0 ES group than in the control group (p < 0.01) of 3T3-L1 adipocytes. In C2C12 cells, the mitochondrial protein voltage-dependent anion channel (VDAC) was significantly increased in the 1.0 ES group (p < 0.01). Furthermore, we found that 1.0 ES activated both 5' AMP-activated protein kinase (AMPK) and acetyl-CoA carboxylase (ACC) in skeletal muscle cells (p < 0.01). [Conclusion] These findings suggest that ES extracts decreased TG content, presumably by increasing lipase in adipocytes and metabolism-associated protein expression as well as mitochondrial biogenesis in muscle cells. These effects may corroborate previous in vivo findings regarding the ergogenic effects of ES supplementation.

Bone Morphogenetic Protein 2-induced MAPKs Activation Is Independent of the Smad1/5 Activation

  • Jun, Ji-Hae;Ryoo, Hyun-Mo;Woo, Kyung-Mi;Kim, Gwan-Shik;Baek, Jeong-Hwa
    • International Journal of Oral Biology
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    • v.34 no.2
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    • pp.115-121
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    • 2009
  • Bone morphogenetic protein (BMP) 2 is a potent osteogenic factor. Although both Smad1/5 and mitogenactivated protein kinases (MAPKs) are activated by BMP2, the hierarchical relationship between them is unclear. In this study, we examined if BMP2-stimulated MAPK activation is regulated by Smad1/5 or vice versa. When C2C12 cells were treated with BMP2, the activation of extracellular signal-regulated kinase (ERK), p38 MAPK and c-Jun-N-terminal kinase was evident within 5 min. The knockdown of both Smad1 and Smad5 by small interfering RNA did not affect the activation of these MAPKs. In addition, neither the overexpression of Smad1 nor Smad5 induced ERK activation. When ERK activation was induced by constitutively active MEK1 expression, the protein level and activation of Smad1 increased. Furthermore, the inhibition of constitutively active BMP receptor type IB-induced ERK activation significantly suppressed Smad1 activation. These results indicate that Smad1/5 activation is not necessary for BMP2-induced MAPK activation and also that ERK positively regulates Smad1 activation.

Molecular Chaperonic Function of C-Reactive Protein Induced by Heating in HT-29 Human Colon Carcinoma Cells

  • Lee, Soo-Young;Jung, Hyun-Jung;Kim, Hyun-Soo;Lee, Seung-Chul;Lee, Si-Back;Joe, Jae-Hoon;Kim, You-Mie
    • BMB Reports
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    • v.33 no.5
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    • pp.407-411
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    • 2000
  • The effects of heat shock, or all-trans retinoic acid, on the expression of the C-reactive protein mRNA in the HT-29 human colon carcinoma cells, as well as the functional role of the C-reactive protein as a molecular chaperone, were studied. The expression level of the C-reactive protein mRNA in the HT-29 cells was increased time-dependently when exposed to heat-shock, and dose-dependently when treated with all-trans retinoic acid. The activities of transglutaminase C and K in the HT-29 cells were significantly increased when treated with all-trans retinoic acid. The C-reactive protein prevented thermal aggregation of the citrate synthase and stabilized the target enzyme, citrate synthase. The C-reactive protein promoted functional refolding of the urea-denatured citrate synthase up to 40-70%. These results suggest that the C-reactive protein, which is induced in human colon carcinoma cells, when heated or treated with all-trans retinoic acid has in a part functional activity of the molecular chaperone.

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