• 제목/요약/키워드: component protein

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인삼 단백성분이 배양한 Chick Embryo의 뇌, 척수, 근육세포에 미치는 효과에 관한 연구 (Studies on the Effect of the Protein Constituents of Panax ginseng Root on Cultured Chick Embryonic Brain, Spinal Cord and Skeletal Muscle Cells)

  • 김영중;한대석;허훈;안상미;구향자
    • 약학회지
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    • 제27권2호
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    • pp.109-116
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    • 1983
  • The effect of protein constituents of six-year old fresh Panax ginseng root on chick embryonic brain, spinal cord and skeletal muscle dissociation cultures was studied. The protein constituents showed the enhancing effect on cultured brain, spinal cord and skeletal muscle cells. The neurite formation from brain and spinal cord cells and the outgrowth of neurite seemed to be enhanced by almost all of the protein constituents employed for this study. The maturation of skeletal muscle cells was stimulated by the protein constituents. This enhancing effect of the protein constituents was more vivid when brain, spinal cord and skeletal muscle cells were cultured with a medium which did not contain chick embryonic extracts known as an essential component for primary cell culture. The protein fraction having molecular weight range of 1,000 to 5,000 out of all the protein fractions employed for this study showed the most stimulatory effect on cultured brain, spinal cord and skeletal muscle cells.

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폐흡충 성충 수용성 단백질의 성분별 생성위치 (Tissue origin of soluble component proteins in salin extract of adult Paragonimus westermani)

  • Yoon Kong;Chi- Yong Park;Shin-Yong Kang;Seung-Yull Cho
    • Parasites, Hosts and Diseases
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    • 제30권2호
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    • pp.91-100
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    • 1992
  • 폐홉충의 생리식염수 추출액 내에 있는 여러 가지 성분 단백질의 생화학적 성상, 면역학적 특징 그리고 충체 내에서의 생성위치 등의 단세포군 항체나 전기영동을 이용한 연구에서 일부 밝혀졌다. 이 실험은 폐흡충 성충의 생리식염수 추출액 내에 있는 각 성분단백질이 폐흡충의 어느 부위에서 유래한 것인지를 알기 위하여 실시하였다. 먼저 생리식염수 추출액을 8% disc-PAGE로 전기영동하여 성분단백질을 분리하고 각 단백질 대(대)를 포함하는 젤을 잘라 내었다. 이어 전기영동으로 젤에서 성분단백질을 용출(용출)하였다. 각각의 단백질을 토끼에 면역시켜 성분 단백질별 항폐흡충 면역혈청을 만들고 이 항혈청으로 폐흡충 및 감염 고양이 폐의 절편에 면역효소 염색법을 시행하였다. 그 결과 성충추출액으로 면역한 항폐흡충 면역혈청은 폐흡충 성충의 충란, 장관상피세포, 장관 내용물에 강한 반응을 보였고 실질조직에도 염색이 되었다. 그러나 표피, 표피하세포, 고환, 흡판등은 반응이 없었다. 1번 Band 단백질의 항혈청은 충란내 세포에 염색이 되었고 충체에서 배출되어 폐실질 조직에 들어있는 충란에 더욱 강하게 반응하였다. 2번 Band 단백질의 항혈청은 폐홉충의 실질조직에 반응하였다. 3번 Band 단백질의 항혈청은 2번 Band 단백질과 교차반응을 일으켜 염색 반응을 관찰하지 않았다. 4번 Band 단백질의 항혈청은 폐흡충의 장관 내용물과 강한 반응을 보였고 5번 Band 단백질의 항혈청은 장관상피세포에 반응하였다. 6/7번 Band 단백질과 8번 나and 단백질의 항혈청은 각각 실질조직에 반응하였다.

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굴(Crassostrea gigas)의 선도에 따른 pH, 글리코겐, 가용성단백질, 탁도와의 상관관계 (Relationship of pH, Glycogen, Soluble Protein, and Turbidity between Freshness of Raw Oyster Crassostrea gigas)

  • 손광태;심길보;임치원;윤나영;서정화;정삼근;정우영;조영제
    • 한국수산과학회지
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    • 제47권5호
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    • pp.495-500
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    • 2014
  • We examined chemical changes in oysters Crassostrea gigas and packing water that were sold after storage at 5, 10, and $20^{\circ}C$. The pH of oysters stored at $5^{\circ}C$ dropped to 5.81 after 10 days of storage, while that of oysters at $10^{\circ}C$ and $20^{\circ}C$ dropped to 5.37 after 8 days and to 5.04 after 4 days, respectively. The glycogen content of oysters stored at $5^{\circ}C$ decreased from 718.89 to 421.85 mg/100g during storage, while that of oysters at $10^{\circ}C$ decreased to 351.49 mg/100 g after 4 days. The turbidity and soluble protein in packing water increased slightly. The viable cell count of oysters did not exceed 6 log CFU/g after 10 days of storage at $5^{\circ}C$, but that of oysters at $10^{\circ}C$ did so after 8 days. Additionally, the viable cell count of packing water was lower than that of oysters. We performed a principal component analysis, where the first principal component (55.03%-57.24%) and second principal component (42.76%-44.97%) described most variation. The first principal component included the pH of oysters and packing water, and the glycogen content of oysters. A Pearson correlation between the first two principal components had a higher R value than that between other components. Freshness was evaluated using the pH of oysters and packing water, and glycogen. We found that soluble protein content was significantly associated with a lower pH and glycogen content.

A System Analysis and Simulation of the Korean Dairy Industry Sector -Milk Supply Component-

  • Lee, Buk-Won
    • 한국경영과학회지
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    • 제4권1호
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    • pp.87-102
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    • 1979
  • In Korea, the traditional main food is rice There is a shortage of food, though the land is uesd intensively. The Koreans produce mainly rice its yield is very much higher than other crops. This leads to the comsumption of one type of food and, hence, to an unbalanced diet. Since 1962, Korean income has been going up rapidly, and the demand for animal protein has also increased. In order to solve the probem, the government decided to develop the dairy industry, because this would enable the population to consume more animal protein, and there is weak competion between rice and milk production.

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Capsaicin, a component of red peppers, stimulates protein kinase CKII activity

  • Rho, Yun-Wha;Bae, Young-Seuk
    • BMB Reports
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    • 제43권5호
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    • pp.325-329
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    • 2010
  • Protein kinase CKII (CKII), a heterotetramer composed of two catalytic ($\alpha$ or $\alpha$') subunits and two regulatory ($\beta$) subunits, plays a critical role in cell proliferation and anti-apoptosis. Recently, capsaicin was shown to trigger apoptosis. Therefore, we examined the effect of capsaicin on CKII activity. Although capsaicin induced apoptotic death in HeLa cells, CKII activity was increased in the cytosolic fraction of HeLa cells after treatment. Capsaicin did not change the expression of the $CKII{\alpha}$ and $CKII{\beta}$ proteins. Capsaicin stimulated the catalytic activity of recombinant CKII tetramer, but not the $CKII{\alpha}$ subunit. Moreover, capsaicin enhanced the autophosphorylation of $CKII{\alpha}$ and $CKII{\beta}$. Taken together, our data suggest that capsaicin stimulates the phosphotransferase activity of CKII holoenzyme by interacting with the $CKII{\beta}$ subunit.

한국산 고등균류 만가닥버섯의 항암성분 (Studies on Constitutents of the Higher Fungi of Korea : Antitumor Components of the Basidiocarps of Hypsizigus mamoreus)

  • 박성미;진미림;김진숙;최응칠;김병각
    • 약학회지
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    • 제37권5호
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    • pp.490-498
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    • 1993
  • To find antitumor components in the hot water extract from the basidiocarps of Hypsizigus mamomus. protein-bound polysaccharides were purified and fractionated by DEAE-cellulose ion exchange column chromatography and Sepharose CL-4B gel filtration chromatography. When a dose of 20 mg/kg/day was injected intraperitoneally into ICR mice. fraction IV of the component showed the highest inhibition ratio of 73.8% against the count of hemolytic plaque forming cells in mice to 3.2 times. when IV was about 30 KD and the fraction was composed of 76.1% polysaccharide and 4.9% protein. The hexosamine was detected in all the fractions, showing that the polysaccharide and protein moieties were bound each other.

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Purification and Characterization of Moran 20K from Morus alba

  • Kim, Eun-Sun;Park, Sung-Jean;Lee, Eun-Ju;Kim, Bak-Kwang;Huh, Hoon;Lee, Bong-Jin
    • Archives of Pharmacal Research
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    • 제22권1호
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    • pp.9-12
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    • 1999
  • A new glycoprotein was purified from the aqueous methanolic extract of the root bark of Morus alba which has been used as a component of antidiabetic remedy in Oriental Medicine. SDS-PAGE result shows that the molecular weight of the glycoprotein was approximately 20 kDa. This new glycoprotein was named as Moran 20K. The protein lowered blood glucose level in streptozotocin-induced hyperglycemic mice model and it also increased the glucose transport in cultured epididymis fat cells. The amino acid composition of the protein was analyzed, and the protein contained above 20% serine and cysteine such as insulin. The actual molecular weight of the protein was determined as 21.858 Da by MALDI-TOF mass spectroscopy.

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Optimized Methods for purification and NMR measurement of antibacterial peptide, bovine lactophoricin

  • Kim, Ji-Sun;Park, Tae-Joon;Kim, Yong-Ae
    • 한국자기공명학회논문지
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    • 제13권2호
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    • pp.96-107
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    • 2009
  • Lactophoricin (LPcin-I) is a cationic amphipathic peptide with 23-mer peptide, and corresponds to the carboxy terminal 113-135 region of Component-3 of proteose-peptone. LPcin-I is a good candidate as a peptide antibiotic, because it has an antibacterial activity, but no hemolytic activity. On the other hand, its shorter analog (LPcin-II), which corresponds to the 119-135 region of PP3, has no antibacterial activity. In order to understand the structure-activity relationship under the membrane environments, we succeed to produce large amounts of LPcin-I and LPcin-II peptides. Peptides were over expressed in the form of fusion protein in Escherichia coli, and purified with several chromatography techniques. In this paper, we introduce the optimizing processes of purification and NMR measurement.

Proteome Analysis of Overproduction of Recombinant Protein in Escherichia coli by Fed-Batch Fermentations

  • 한미정;최종현;정기준;유종신;이상엽
    • 한국생물공학회:학술대회논문집
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    • 한국생물공학회 2001년도 추계학술발표대회
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    • pp.750-753
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    • 2001
  • Proteomics is a formalized approach for obtaining a rapid snap-shot of the protein complement of a tissue, cell or cell component. Such an approach is powerful in that it allows a parallel assessment of temporal protein fluxes. This is an important concept in view of the dynamic nature of protein expression. Undoubtedly, changes in protein expression are essential in any study aimed at investigating cellular networks. In this study, we analyzed and compared the proteomes of recombinant E. coli strain before and after induction. Proteome expression patterns of recombinant E. coli were resolved on 2D-gels, and the variations in the relative expression level of particular proteins were examined using software-aided protein quantification tool. We observed above 800 spots on a 2D-gel using Melanie II software. Many proteins which involved in chaperones were significantly up-regulated in recombinant E. coli. Therefore, it could be concluded that the expression of recombinant protein in E. coli acted as a stress to the cells, which change cells ability to synthesize proteins and induced the expression of various protective proteins.

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Effects of Feeding Betaine on Performance and Hormonal Secretion in Laying Hens

  • Park, Jae-Hong
    • 한국가금학회:학술대회논문집
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    • 한국가금학회 2006년도 제23차 정기총회 및 학술발표회
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    • pp.17-27
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    • 2006
  • The effects of dietary betaine on performance, blood compositions, hepatic amino acid concentrations and hormonal secretions were examined in laying hens. Egg production was significantly higher in birds fed the 16.5 % protein diet compared to those fed 14.5 % protein diet(p<0.05), whereas dietary supplementation of betaine did not show any significant effect. The high level of protein and betaine supplementation significantly improved egg weight, egg mass and feed conversion(p<0.05), while eggshell breaking strength, eggshell thickness and Haugh unit were not influenced by betaine and dietary protein levels. Supplemental betaine did not affect serum total protein, albumin and BUN concentration. However, uric acid concentration significantly increased in 600 ppm betaine-fed groups(p<0.05). Concentrations of most hepatic amino acid were influenced by increased protein feeding and dietary betaine supplementation. Hormone studies recorded significantly higher serum and hepatocyte IGF-I concentration in 600 and 1,200 ppm betaine treatments(p<0.05) compared to those of control group. IGF-I mRNA gene expression of hepatocytes revealed statistically correlated increase in 600 and 1,200 ppm betaine-fed groups compared to the controls(p<0.05). Serum IGFBP-3 concentration was significantly elevated in 600 ppm betaine treatments. However, the secretion of IGFBP-1 in hepatocyte of laying hens fed with 600 and 1,200 ppm of betaine showed a significant decrease compared to the control group(p<0.05). Results of these study show that dietary betaine supplementation affects protein and hormone metabolism in laying hens.

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