• Title/Summary/Keyword: C5 protein

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The Activity and Characteristics of $\alpha$-Amylase Present in Soy Milk and Jeungpyun Batters (증편 제조시 콩물과 반죽 내의 $\alpha$-amylase활성 및 특성에 관한 연구)

  • Na, Han-Na;Yoon, Sun;Kim, Jung-Soo;Kim, Bo-Young
    • Korean journal of food and cookery science
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    • v.14 no.3
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    • pp.261-265
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    • 1998
  • The activity and characteristics of ${\alpha}$-amylase in soy milk as well as in Jeungpyun batters were determined to investigate the enzyme system related to Jeungpyun preparation. ${\alpha}$-Amylase activity was detected in soy milk as well as in Jeungpyun batters. Soy milk had ${\alpha}$-amylase activity of 0.79 units/mg protein for gelatinized starch and 0.036 units/mg protein for raw starch. ${\alpha}$-Amylase in soy milk showed maximum activities at pH 5.92∼6.87 and at 60$^{\circ}C$ for both gelatinized starch and raw starch. ${\alpha}$-Amylase activities of Jeungpyun batters containing soy milk were 25.59 units/mg protein for gelatinized starch and 1.37 units/mg protein for raw starch. Jeungpyun batters without soy milk demonstrated ${\alpha}$-amylase activities of 3.37 units/mg protein for gelatinized starch and 0.49 units/mg protein for raw starch. ${\alpha}$-Amylase of Jeungpyun batters showed an optimal activity at pH 5.25 and at 60$^{\circ}C$ for both gelatinized and raw starch. The results demonstrated that Jeungpyun batters with soy milk showed significantly higher ${\alpha}$-amylase activity than the ones without soy milk.

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Effects of cranberry powder on serum lipid profiles and biomarkers of oxidative stress in rats fed an atherogenic diet

  • Kim, Mi-Joung;Jung, Ha-Na;Kim, Ki-Nam;Kwak, Ho-Kyung
    • Nutrition Research and Practice
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    • v.2 no.3
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    • pp.158-164
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    • 2008
  • This study investigated that the antioxidative effect of freeze-dried cranberry powder against protein and lipid oxidation and ameliorative effect of serum lipid profile in rat fed atherogenic diet. Six weeks old male Sprague-Dawley rats were divided into the following four groups: normal diet group with 5% com oil(control), atherogenic diet group with 5% com oil, 10% lard, 1% cholesterol, and 0.5% sodium cholate(HFC), atherogenic plus 2% cranberry powder diet group(HFC+C2), and atherogenic plus 5% cranberry powder diet group(HFC+C5), and respective diet and water were fed daily for 6 weeks. After the experimental period, the serum lipid profile, such as total cholesterol, HDL-cholesterol, LDL-cholesterol, and triglyceride, ferric reducing ability of plasma(FRAP), plasma phenolics content, superoxide dismutase(SOD) activity, serum protein carbonyl and thiobarbituric acid reactive substances(TBARS) levels were examined. Total phenolic compound and total flavonoid levels in freeze-dried cranberry powder were 9.94 mg/g and 8.12 mg/g, respectively. Serum total cholesterol and LDL-cholesterol levels were not significantly different for cranberry powder treatment, but serum HDL-cholesterol level was significantly increased in HFC+C5 group compared with HFC group. Plasma FRAP value tended to be increased by cranberry powder treatment though there was no significant difference. Plasma total phenol concentrations and SOD activities were not significantly different among all groups. Serum protein carbonyl and TBARS levels were significantly decreased in HFC+C5 group compared with HFC group. Overall results suggested that freeze-dried cranberry powder might have the serum lipid improving effect, as well as anti oxidative effect demonstrated by its protective effect against protein and lipid oxidation.

Expression of Fusion Products of Insecticidal Crystal Protein Genes from Two Different Bacillus thuringiensis Strains (두종의 Bacillus thuringiensis 내독소단백질 유전자의 융합에 의한 발현)

  • 제연호;김상현
    • Journal of Sericultural and Entomological Science
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    • v.35 no.1
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    • pp.36-42
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    • 1993
  • Expression of insecticidal protein by fusion product of truncated HD-1[CryIA(a)] N-terminal and HD-73[CryIA(c)] C-Terminal fragment of Bacillus thruingiensis subsp. kurstaki was investigate. Immunological analysis of transformants by using polyclonal antisera raised against the whole-crystal protein of HD-1 revealed that SK4 and SK5 were observed cross-reaction with polypeptides of 77-kDa and 105-kDa, respectively. Bioassay of the transformant pSK5 to Plutella maculipennis and Heliothis assulta were 96% and 97%, respectively.

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Transcriptional Modulation of Metabolism-Related Genes in Brackish Water Flea Diaphanosoma celebensis Exposed to Mercury (수은 노출에 따른 기수산 물벼룩의 대사 관련 유전자의 발현 양상)

  • Min Jeong, Jeon;Je-Won, Yoo;Young-Mi, Lee
    • Journal of Marine Life Science
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    • v.7 no.2
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    • pp.145-153
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    • 2022
  • Mercury (Hg) is a major concern in marine environment because of their bioaccumulation and biomagnification properties, and adverse effects to aquatic organisms at even a trace amount. However, little information on the effects of Hg, compared to other heavy metals, is available in marine small crustaceans. Here, we investigated the transcriptional modulation of metabolism-related genes in the brackish water flea, Diaphanosoma celebensis after exposure to sublethal concentration (0.2, 0.4, 0.8 ㎍/l) of HgCl2 for 48 h. Relative mRNA expression levels of five detoxification enzyme-coding genes (cytochrome P450; cyp360A1, cyp361A1, cyp4AP3, cyp4C122, and cyp370C5) and six digestive enzyme-coding genes [alpha amylase (AMY), alpha amylase related protein (AMY-like), trypsin (TRYP), chymotrypsin-like protein (CHY), lipase (LIP), pancreatic lipase-related protein (PLRP)] were analyzed using quantitative real time reverse transcription polymerase chain reaction (qRT-PCR). As results, Hg increased the mRNA level of cyp370C5 (clan2) and cyp4AP3 (clan4) in a concentration dependent manner. A significant increase in TRYP mRNA was also concentration-dependently observed after exposure to Hg. These findings suggest that cyp370C5 and cyp4AP3 play a key role in Hg detoxification in D. celebensis, and Hg can affect energy metabolism by modulating the transcription of digestive enzyme. This study will provide better understanding the molecular effects of Hg in marine small crustacean.

Extraction of protein from defatted sesame meal using the enzyme from Bacillus sp. CW-1121 (Bacillus sp. CW-1121이 생성하는 단백 분해 효소를 이용한 참깨박 단백질의 용출)

  • Choi, C.;Chun, S.S.;Cho, Y.J.
    • Applied Biological Chemistry
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    • v.36 no.2
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    • pp.121-126
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    • 1993
  • To extract insoluble proteins of sesame meal residue by using microorganism, the sesame meal residue was treated with crude enzyme solution from Bacillus sp. CW-1121. It was found that the solubility reached to maximum at pH 7.5, $45^{\circ}C$. Under optimum condition, the nitrogen solubility with the enzyme solution from Bacillus sp. CW-1121 reached to 60% in 2 hours. Nitrogen solubility of protein from sesame meal showed minimum value at pH 4.5 and significantly increased above pH 6.0. When the protein from sesame meal extracted with Bacillus sp. CW-1121 was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis, water soluble protein was showed 4 bands and salt soluble protein was showed 2 bands. The amino acid composition of water soluble protein, salt soluble protein and free amino acid indicated relatively high contents of serine (17.24 mg/g), glutamic acid (10.77 mg/g) and glutamic acid (6.55 mg/g). Specially, the contents of essential amino acids were high.

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Evaluating Nutritional Quality of Single Stage- and Two Stage-fermented Soybean Meal

  • Chen, C.C.;Shih, Y.C.;Chiou, P.W.S.;Yu, B.
    • Asian-Australasian Journal of Animal Sciences
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    • v.23 no.5
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    • pp.598-606
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    • 2010
  • This study investigated the nutritional quality of soybean meal (SBM) fermented by Aspergillus ($FSBM_A$) and/or followed by Lactobacillus fermentation ($FSBM_{A+L}$). Both fermented products significantly improved protein utilization of SBM with higher trichloroacetic acid (TCA) soluble true protein content, in vitro protein digestibility and available lysine content, especially in $FSBM_{A+L}$. Moreover, $FSBM_{A+L}$ produced a huge amount of lactic acid resulting in lower pH as compared to the unfermented SBM or soybean protein concentrate (SPC) (p<0.05). $FSBM_A$ and $FSBM_{A+L}$ raised 4.14% and 9.04% of essential amino acids and 5.38% and 9.37% of non-essential amino acids content, respectively. The ${\alpha}$-galactoside linkage oligosaccharides such as raffinose and stachyose content in $FSBM_A$ and $FSBM_{A+L}$ decreased significantly. The results of soluble protein fractions and distribution showed that the ratio of small protein fractions (<16 kDa) were 42.6% and 63.5% for $FSBM_A$ and $FSBM_{A+L}$, respectively, as compared to 7.2% for SBM, where the ratio of large size fractions (>55 kDa, mainly ${\beta}$-conglycinin) decreased to 9.4%, 5.4% and increased to 38.8%, respectively. There were no significant differences in ileal protein digestibility regardless of treatment groups. SPC inclusion in the diet showed a better protein digestibility than the SBM diet. In summary, soybean meal fermented by Aspergillus, especially through the consequent Lactobacillus fermentation, could increase the nutritional value as compared with unfermented SBM and is compatible with SPC.

The Mechanism of Poly I:C-Induced Antiviral Activity in Peritoneal Macrophage

  • Pyo, Suh-Kenung
    • Archives of Pharmacal Research
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    • v.17 no.2
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    • pp.93-99
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    • 1994
  • Macrtophages play an important role in defense against virus infection by intrinsic resistance and by extrinsic resistance. Since interferon-induced enzymes which are 2'-5' oligoadenylate synthetase and p1/eIF-2 protein kinase have been shown to be involved in the inhibition of viral replication, I examined the mechanism by which poly I:C, an interferon inducer, exerts its antiviral effects in inflammatory macrophages infected with herpes simplex virus type 1 (HSV-1). The data presented here demonstrate that poly I:C-induced antiviral activity is partially due to the activation of 2'-5' pligoadenylate synthetase. The activation of 2'-5' oligoadenlate A synthetase by poly I:C is also at least mediated via the production of interferon-.betha.. Taken together, these data indicate that interferon-.betha. produced in response to poly I:C acts in an autocrine manner to activate the 2'-5' oligoadenylate synthetase and to induce resistance to HSV-1.

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Activity of Protein Kinase C in Abnormally Proliferated Vascular Endothelial Cells (비정상적인 세포증식이 유도된 혈관 내피세포에서 Protein Kinase C에 대한 활성 분석)

  • Bae, Yong Chan;Park, Suk Young;Nam, Su Bong;Moon, Jae Sul;Choi, Su Jong
    • Archives of Plastic Surgery
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    • v.34 no.1
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    • pp.13-17
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    • 2007
  • Purpose: To understand the pathogenesis of the disease that presents abnormally proliferated vascular endothelial cells, a model of DMH(1,2-dimethylhydrazine)-induced abnormal proliferation of HUVECs(Human Umbilical Vein Endothelial Cells) was made. We indirectly determined that Protein Kinase C(PKC) restricts the cellular proliferation and inhibits the manifestation of growth factor by using several inhibiting substances of the transmitter through our previous studies. Thereupon, we attempted to observe direct enzymatic activities of PKC and its correlation with the abnormal proliferation of vascular endothelial cells. Methods: $10^5$ HUVECs cells were applied to 6 individual well plates in three different groups; A control group cultured without treatment, a group concentrated with $0.75{\times}10^{-8}M$ DMH only, and a group treated with DMH & $5{\times}10^{-9}M$ Calphostin C, inhibitor of PKC. In analyzing the formation of intracellular PKC enzyme, protein separation was performed, and separated protein was quantitatively measured. PKC enzyme reaction was analyzed through Protein Kinase C Assay System (Promega, USA), and the results were analyzed according to Beer's law. Results: Enzymatic activity of PKC presented the highest in all reaction time of a group concentrated only with DMH, and the lowest in the control group. The group treated with DMH and the inhibitor revealed statistically lower enzymatic activity than group only with DMH in all reaction time, although higher than the control group. Conclusion: From the enzymatic aspect, most active and immediate reaction of the PKC was observed in the group concentrated with DMH only. The group treated with DMH & PKC inhibitor showed meaningful decrease. Accordingly, PKC holds a significant role in DMH-induced abnormal proliferation of vascular endothelial cells.

Bacterial ${\beta}$-Lactamase Fragment Complementation Strategy Can Be Used as a Method for Identifying Interacting Protein Pairs

  • Park, Jong-Hwa;Back, Jung-Ho;Hahm, Soo-Hyun;Shim, Hye-Young;Park, Min-Ju;Ko, Sung-Il;Han, Ye-Sun
    • Journal of Microbiology and Biotechnology
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    • v.17 no.10
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    • pp.1607-1615
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    • 2007
  • We investigated the applicability of the TEM-l ${\beta}$-lactamase fragment complementation (BFC) system to develop a strategy for the screening of protein-protein interactions in bacteria. A BFC system containing a human Fas-associated death domain (hFADD) and human Fas death domain (hFasDD) was generated. The hFADD-hFasDD interaction was verified by cell survivability in ampicillin-containing medium and the colorimetric change of nitrocefin. It was also confirmed by His pull-down assay using cell lysates obtained in selection steps. A coiled-coil helix coiled-coil domain-containing protein 5 (CHCH5) was identified as an interacting protein of human uracil DNA glycosylase (hUNG) from the bacterial BFC cDNA library strategy. The interaction between hUNG and CHCH5 was further confirmed with immunoprecipitation using a mammalian expression system. CHCH5 enhanced the DNA glycosylase activity of hUNG to remove uracil from DNA duplexes containing a U/G mismatch pair. These results suggest that the bacterial BFC cDNA library strategy can be effectively used to identify interacting protein pairs.

APP Tail 1 (PAT1) Interacts with Kinesin Light Chains (KLCs) through the Tetratricopeptide Repeat (TPR) Domain (APP tail 1 (PAT1)과 kinesin light chains (KLCs)의 tetratricopeptide repeat (TPR) domain을 통한 결합)

  • Jang, Won Hee;Kim, Sang-Jin;Jeong, Young Joo;Jun, Hee Jae;Moon, Il Soo;Seog, Dae-Hyun
    • Journal of Life Science
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    • v.22 no.12
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    • pp.1608-1613
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    • 2012
  • A conventional kinesin, KIF5/Kinesin-I, transports various cargoes along the microtubule through interaction between its light chain subunit and the cargoes. Kinesin light chains (KLCs) interact with many different cargoes using their tetratricopeptide repeat (TPR) domain, but the mechanism underlying recognition and binding of a specific cargo has not yet been completely elucidated. We used the yeast two-hybrid assay to identify proteins that interact with the TPR domain of KLC1. We found an interaction between the TPR domain of KLC1 and an amyloid precursor protein (APP)-binding protein PAT1 (protein interacting with APP tail 1). The yeast two-hybrid assay demonstrated that the TPR domain-containing region of KLC1 mediated binding to the C-terminal tail region of PAT1. PAT1 also bound to KLC2 but not to kinesin heavy chains (KIF5A, KIF5B, and KIF5C) in the yeast two-hybrid assay. These protein-protein interactions were also observed in the glutathione S-transferase (GST) pull-down assay and by co-immunoprecipitation. Anti-PAT1 antibody as well as anti-APP anti-body co-immunoprecipitated KLC and KHCs associated with PAT1 from mouse brain extracts. These results suggest that PAT1 could mediate interactions between Kinesin-I and APP containing vesicles.