• Title/Summary/Keyword: Protein C

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Environmental factors regulating the expression of Porphyromonas gingivalis heat shock protein (Porphyromonas gingivalis의 열충격단백 발현조절 환경인자에 관한 연구)

  • Choi, Jeom-Il
    • Journal of Periodontal and Implant Science
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    • v.34 no.1
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    • pp.29-33
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    • 2004
  • The present study was done to evaluate the environmental factors responsible for the expression of Porphyromonas gingivalis heat shock protein. The intensity of the heat shock protein gene expression was comparable to those seen by the heat shock ptreatment of the bacteria $(44^{\circ}C)$ when the bacteria was grown as a mixed culture or biofilm state at $37^{\circ}C$.

Gene Expression in The Fifth Generation of TMV Resistant Transgenic Tobacco Plane at Elevated Temperature (TMV 저항성 형질전환 연초식물체 제 5 세대에서 유전자 안정성 및 고온조건에서의 유전자 발현)

  • 이기원;박성원;이청호;박은경;김상석;최순용
    • Korean Journal of Plant Tissue Culture
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    • v.25 no.4
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    • pp.245-250
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    • 1998
  • Tobacco mosaic virus(TMV) coat protein cDNA was transformed to Nicotiana tabacum cv. NC82 and the transgenic tobacco plants resistant to TMV infection were isolated in the next generation. The expression of TMV coat protein cDNA and genetic stability of the fifth generation of TMV resistant transgenic tobacco plants at the higher temperature were investigated. The TMV coat protein cDNA was amplified by genomic PCR in all the TMV resistant transgenic tobacco plants. The TMV coat protein expressed in the transgenic tobacco plants was detected at very low level by immunoblot hybridization. Even in tansgenic plants that showed the viral symptom only on very late sucker growth (delay type plants), the coat protein expression in the suckers was much less than that of susceptible tobacco infected with TMV. The TMV coat protein expressed in the transgenic tobacco plants was below 0.01% of total protein. Transcription and expression of the coat protein cDNA in delay type plants were observbed at high temperature (38$^{\circ}C$), and TMV replication was suppressed at both 28$^{\circ}C$ and 38$^{\circ}C$. This indicates that unlike the resistance conferred by 'N' gene. TMV resistance of transgenic tobacco plant won't break down at high temperature.

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Immunohistochemical c-fos Expression in Osteosarcoma (골육종의 c-fos 발현에 관한 면역조직화학적 검색)

  • Park, Yong-Koo;Park, Hye-Rim
    • The Journal of the Korean bone and joint tumor society
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    • v.5 no.3
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    • pp.162-168
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    • 1999
  • The products of c-fos and c-jun proto-oncogenes form the heterodimeric complex activator protein 1 (AP-1), which plays an important part in the control of bone cell proliferation and differentiation, as well as in the development of bone tumors. The expression of c-fos protein was examined in 35 cases of human osteosarcomas as formalin-fixed paraffin-embedded tissue sections using a monoclonal antibody. The expression of c-fos was restricted to bone-forming lesions, while low grade cartilaginous tumors were devoid of immunoreactivity. The highest levels of c-fos expression were detected in osteoblastic osteosarcoma (13 of 17 cases with grade one on two) while two chondroblastic osteosarcomas, one fibroblastic osteosarcoma, and two parosteal osteosarcomas were negative. Two cases of telangiectatic osteosarcomas were positive for c-fos protein. However, since there is a tendency of high c-fos protein expression at the higher histological grade, significant differences were not present in the expression of c-fos protein. Thus c-fos expression may be implicated in the development of osteosarcomas, but they appear to have little or no relevance in the development of low grade cartilaginous neoplasms.

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Optimum Drying Condition for Slaughter Porcine Blood and Its Utilization as Broiler Diets (돈혈의 적정 건조조건과 육계사료로서의 재활용 방안)

  • 박강희
    • Korean Journal of Poultry Science
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    • v.24 no.2
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    • pp.59-66
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    • 1997
  • Optimum drying conditions to utilize porcine blood from slaughter house for blood meals, and the effects of blood meals on growth in broiler chicks were investigated. Moisture and protein con-tents of slaughter porcine blood were 79.8 and 16.4%, respectively. The protein contents of the flash dried blood meals at 80˚C were not different from those of the spray dried blood meals at 160 and 190˚C, but higher by 17% relative to those of the spray dried blood meals at 80 and 120˚C. Results from protein analysis by SDS-polyacrylamide electrophoresis showed that flash dried blood meals at 80˚C and spray dried blood meals at 160˚C were better than spray dried blood meals at 80, 120 and 190˚C in terms of protein quality. In Feeding Trial I with broiler chicks, body weights of chicks fed 2, 4 and 6% flash dried blood meal diets at 80˚C were increased at 35 days by 5.6, 7.9 and 4.0%, respectively, compared to control group(P<0.05). In Feeding Trial II, body weights of chicks fed 4 and 6% flash dried blood meal diets at 80˚C were increased at 42 days by 4.9 and 5.3%, respectively, compared to control group(P<0.05). Feed conversion ratios of chicks fed diets 4 and 6% flash dried blood meal diets at 80˚C were significantly improved at 42 days by 7.0 and 3.7%, respectively, compared to that of control group(P<0.05). The optimum drying condition of slaughter porcine blood seemed to be the flash drying method at 80˚C

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Construction of Recombinant Xanthomonas campestris Strain Producing Insecticidal Protein of Bacillus thuringiensis

  • Shin, Byung-Sik;Koo, Bon-Tag;Choi, Soo-Keun;Park, Seung-Hwan
    • Journal of Microbiology and Biotechnology
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    • v.4 no.4
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    • pp.285-289
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    • 1994
  • An insecticidal crystal protein gene, cryIA(c), from Bacillus thuringiensis HD-73 was integrated into the chromosome of a xanthan-producing bacterium, Xanthomonas campestris XP92. The cryIA(c) gene expression cassette was constructed that placed the gene between the trc promoter and rrnB transcriptional terminator. The $lacl^q$ gene was also included to prevent the expression of cryIA(c) gene in X campestris cells. Southem blot analysis confirmed the integration of the cryIA(c) gene expression cassette in chromosome of X campestris XP92 transconjugant. Expression of the insecticidal crystal protein was confirmed by Western blot analysis and bioassay against the larvae of Hyphantria cunea (Lepidoptera: Arctiidae) and Plutella xylostella (Lepidoptera:Plutellidae).

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Inhibitory Activity against Protein Kinase C of Some Medicinal Plants (수종 생약의 Protein kinase C 저해활성)

  • Lee, Hyun-Sun;Ahn, Soon-Cheol;Kim, Bo-Hyun;Park, Moon-Su;Oh, Won-Keun;Yoon, Byung-Dae;Ahn, Jong-Seog;Mheen, Tae-Ick
    • Korean Journal of Pharmacognosy
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    • v.23 no.3
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    • pp.142-145
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    • 1992
  • MeOH extract of twenty medicinal herbs were screened for their effects against protein kinase C (PKC) using bleb-forming assay and PKC enzyme assay. Smilax china and Sanguisorba officinalis showed potent anti-PKC activity. Campsis grandiflora and Galla Halepensis showed moderate inhibitory effect on PKC.

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Translocation of Seed Storage Proteins into Microsomes Isoalted from Rice Endosperm Cells

  • Kim, Woo Taek
    • Journal of Plant Biology
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    • v.37 no.3
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    • pp.293-299
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    • 1994
  • Developing rice endosperm cells display two morphologically distinct rough endoplasmic reticulum (ER) membranes, the cisternae ER (C-ER) and theprotein body ER (PB-ER), the latter delimiting the prolamine protein bodies. We (Li et al., 1993) have recently shown that the storage protein mRNAs are not randomly distributed on these ER types; the C-ER is enriched for glutelin mRNAs, whereas the PB-ER harbors predominantly prolamine transcripts. To address whether these ER types have differnet capacities to translate these mRNAs and translocate their proteins into the lumen, a microsomal fraction enriched in C-ER vesicles was prepared from devleoping rice seeds. When present in an in vitro translatin system, the microsomes were able to proteolytically remove the signal peptide and internalize both preproglutelin and preprolamine within the microsomal vesicles. Of the two species, preprolamine was more effectively translocated and processed. These results suggest that the C-ER has the capacity to recognize and bind both storage protein mRNAs during protein synthesis. Moreover, efficient translocation and processing of glutelin requires additional factors that are deficient or absent in the in vitro system.

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A study on short-term stability of recombinant protein A (Recombinant protein A의 short-term stability에 관한 연구)

  • Kim, Yoo-Gon;Lee, Woo-Jong;Won, Chan-Hee;Kim, Yong-Hee;Yun, Ji-Sun;Hong, Min-Seon;Shin, Chul-Soo
    • Analytical Science and Technology
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    • v.24 no.3
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    • pp.193-199
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    • 2011
  • The purpose of this experiment is to evaluate the stability of products according to the storage methods, the period of use, and the diurnal variations through the short term stability experiment of recombinunt protein A (rProtein A) produced in AP Tech Co. That is, we investigated how long the stability of the products would last, when we used the samples frozen at $-20^{\circ}C$, which is one of the storage conditions of the produced rProtein A and then kept them refrigerated at $4^{\circ}C$. The experiment was conducted for 8 weeks and 6 experiment points were established. The experiment was done by thawing the samples frozen at $-20^{\circ}C$ at room temperature, and then refrigerating them at $4^{\circ}C$. In addition, experiments for endotoxin, bioburden, HPLC purity, and concentration were conducted. As a result of the experiment, 0.5 EU/mg endotoxin was detected both at the beginning and at the 8th week and bioburden was not analyzed. In the case of purity, it showed 99.23~99.90% at 210 nm (RSD% 0.23%) and 100% at 280 nm, which meant the change into other materials didn't happen and there was no material degradation characteristics. Finally, we also found the fact that the concentration stayed stable at 55.15 mg/mL (RSD% 0.55%) both at the beginning and at the end. From the experiment results, we were able to conclude that the stability at the condition to store rProtein A at 4 oC for 8 weeks was procured without producing microorganisms or having material degradation characteristics.

The Study on The Nutritional Status of The Packed Lunch Boxes for Junior High School Students in Seoul City (서울시내(市內) 중학생(中學生)의 도시락 영양(營養) 실태조사(實態調査))

  • Chang, Myung-Sook
    • Journal of Nutrition and Health
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    • v.6 no.2
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    • pp.35-43
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    • 1973
  • This study is concerned with the nutritional status of the packed lunch boxes which are brought by the junior high school students in Capital City of Seoul. Four hundred and eights students of the 8 school districts in Seoul had been randomly selected as subjects. The contained nutrients in the packed lunch were analysed by the Food Composition Table. To observe the influence of home economical status and mother's educational level on the nutrient concents of packed lunches, the chosen subjects were classified into three large groupings, which are upper, middle and low classes respectively. In addition, comparison between the Recommended Daily Allowanced for Korean people-13 to 15 age group-and the contained nutrients in the lunch boxed had been conducted. T-test was applied to clarify the significance of the differences between each group both economical and educational level. 1. The averaged rations between the Recommended Daily Allowances and the contained nutrients in the lunches stand: Calorie 59.7% (566 Cal.) protein 53.1% (18g), animal protein 48.6% (5g), fat 39.8% (5g), calcium 371.% (0.1g), ferret 66.4% (2.9g) Vitamin A 642 1.U. (31.3%), Vitamin $B_1$ 70.2% (0.3mg), Vitamin $B_2$ 41.4% (0.2g), Niacin 77.0%(4mg), Vitamin C 51.9% (13mg). All of the nctrients fall far behind the Recommended Daily, Allowances for 13 to 15 age group. 2. Home economical status brings influence on the kinds of foods which could been. Protein, animal protein, fat, Vitamin $B_2$, Vitamin C showed significance of diffierences between the upper and middle classes. Between the middle and low classes, Protein, animal protein, fat, calcium and Vitamin C showed significance of difference. And finally, between the upper and low classes, protein, fat, calcium, ferret, Vitamin $B_2$ and Vitamin C showed a great significance. 3. Regardless to the living conditions of the subject students, all the nutrients of the lunches packed by the mothers in the entire educational levels did not reach the Recommended Daily Allowances. Protein, animal protein, fat, ferret, Vitamin A, and Niacin showed the significance of the differences between the upper and middle classes. On the other hand, calorie, animal protein, fat, Vitamin A and Vitamin C showed the significance between the middle and low classes. Between the upper and the low classes, protein, animal protein, fat, and ferret showed significance. 4. The mairdish-ice of the lunch boxes supplied calorie, protein, Vitamin $B_1$, Vitamin $B_2$ and Niacin which stand at 83.8%, 56.1%, 52.5%, and 54.8% respectivly when compared with the whole nutritional contents. 5. The side-dishes of the packed lunch lack in variety of cooking methods. One interesting fact is that entire subject students are very favorable to the food cooked with every kind of grains.

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Effects of the Protein Fraction of Panax ginseng on Primary Cultured Chicken Brain Cells and DRG (인삼 단백분획물이 일차배양한 계배의 뇌세포 및 DRG에 미치는 영향)

  • Park, Mi-Jung;Song, Jin-Ho;Kim, Sun-Yeou;Kim, Young-Choong
    • YAKHAK HOEJI
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    • v.34 no.5
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    • pp.365-373
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    • 1990
  • The effects of the protein fraction of Panax ginseng on primary cultured chicken embryonic brain cells and DRG cultured with a deficient medium were studied. The protein fraction was further fractionated into four groups according to the molecular weight; larger than 10,000 dalton(fraction A), between 5,000 and 10,000 daltons(fraction B), between 1,000 and 5,000 daltons(fraction C), between 500 and 1,000 daltons(fraction D). All four protein fractions at the concentration of $100\;{\mu}g/ml$ significantly increased the number of the brain cells which promoted the neurite outgrowth. The activity of PDHC in the brain cells was elevated significantly by the protein fraction B at the concentration of $100\;{\mu}g/ml$. It was noted that $100\;{\mu}g/ml$ protein fraction C and D significantly enhanced the synthesis of protein in the brain cells. At the concentration of $100\;{\mu}g/ml$, the protein fraction B enhanced RNA synthesis and the protein fraction A significantly enhanced DNA synthesis in the brain cells. The protein fractions B, C, and D significantly promoted the neurite outgrowth of DRG at the concentration of $100\;{\mu}g/ml$.

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