• Bioindustry News
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• v.13 no.3
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• pp.18-19
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• 2000

• 대한치주과학회:학술대회논문집
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• 2007.11a
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• pp.122-122
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• 2007

• Journal of Life Science
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• v.5 no.2
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• pp.34-34
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• 1995

• The Microorganisms and Industry
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• v.35 no.2
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• pp.2-6
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• 2009

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.91-92
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• 2000

• Journal of dental hygiene science
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• v.11 no.1
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• pp.55-61
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• 2011

The purpose of this study was to investigate the biological function of ODAM and its signal transduction pathway in the steps of ameloblast differentiation and enamel mineralization. An ODAM recombinant protein was produced and stable ODAM transgenic cell lines were also established using ameloblast-lineage cells (ALCs). To verify the ODAM signal transduction pathway, BAMBI recombinant protein, an inhibitor of BMP2 and BMP receptor 1B (BMPR-1B), was treated and BMPR-1B siRNA was used to silence expression of BMPR-1B. Mineralization was augmented by the ALCs treated with the ODAM recombinant protein and the sense ODAM overexpressing cells. The ALP activity was also increased markedly in the sense ODAM overexpressing cells and the ALCs treated with ODAM recombinant protein. The inactivation of ODAM in the ALCs down-regulated the expression of BMPR-1B, whereas its expression was up-regulated markedly when ODAM was overexpressed. These results provide deeper insights into the process of ameloblast maturation and in enamel mineralization. It also suggested that ODAM augmented enamel mineralization.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.22 no.6
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• pp.542-549
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• 2021

The purpose of this study was to provide an economical and easy preparation method for recombinant human epidermal growth factor (rhEGF) without the need for an expensive enzyme to cleave the fusion part. However, the N-terminal fusion part is still useful for affinity chromatography. The hEGF is an important hormone in cell growth and proliferation in humans, and many studies on the expression and purification of this protein have been reported. In the present study, the hEGF gene was designed to be optimized with the E. coli codon usage preference and to contain Asn-Gly at the N-terminus of the protein. The gene was inserted into pRSET_A, an E. coli expression vector, and transformed into E. coli BL21 (DE3). The recombinant fusion protein was successfully co-expressed with pG-Tf2, a chaperone vector, in E. coli and purified by Ni-NTA column chromatography. The rhEGF was then released by hydroxylamine treatment and confirmed by SDS-PAGE. ELISA analysis showed that the activity of the free rhEGF was more than 92% similar to that of commercial EGF. The biological activity of the rhEGF was confirmed by a cell proliferation test with human skin fibroblasts.

• Journal of Life Science
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• v.20 no.10
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• pp.1427-1432
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• 2010

This study was carried out to evaluate neutralization effects against WSSV using antiserum produced from recombinant envelop protein, rVP466 of WSSV. The VP466 gene of WSSV was cloned into pCold I expression vector and rVP466 was expressed in E. coli RIPL. The antiserum against rVP466 was produced in white rabbits (New Zealand white rabbit). The specific immunoreactivity to the antigen, rVP466, was confirmed by Western blot. The constant amounts of WSSV at $1{\times}10^4$ diluted stocks were mixed with various antiserum concentrations and then injected to the muscle of shrimp, Penaeus chinensis, for the neutralization challenge. The shrimps challenged with WSSV as a positive control and those with the mixture of WSSV and preimmune serum as a preimmune control showed 100% cumulative mortality at 17 days post challenge and 83% at 25 days post challenge, respectively. The shrimps challenged with 3 different mixtures of WSSV and rVP466 antiserum at ratios of 1:0.01, 1:0.1 and 1:1 showed 73%, 53% and 46% cumulative mortalities at 25 days post challenge, respectively. These results indicated that WSSV could be neutralized by the rVP466 antiserum. These results suggest that envelop protein VP466 is involved in the initial step of WSSV infection in shrimp.

• The Microorganisms and Industry
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• v.16 no.2
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• pp.62-66
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• 1990

생물공정의 개념을 단백질, 탄수화물, 지방등의 생물질을 동물, 식물, 미생물의 자원으로부터 생산하기 위한 과정의 집합체로 정의 한다면 매우 광범위하며 이에 대해 본 고에서와 같이 작은 글에서 논한다는 것은 불가능에 가깝다 하겠다. 더욱이 생물공정을 산업화하기 위한 공장설계의 단계로 넘어간다면 예를 들어 한정된 경우에 대해 설명할 수 밖에 없겠다. 따라서 본 고에서 재조합 단백질의 정제 공정과 이것의 공정설계에 있어 고려할 점을 논술함으로써 생물공정과 공장설계의 한 단면을 조감하였으면 한다.

• Korean Chemical Engineering Research
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• v.57 no.1
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• pp.85-89
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• 2019

Cell-free protein synthesis utilizes the translational machinery in a cell extract. Unlike the conventional cell-based expression methods, not being affected by the conditions for cell growth, cell-free protein synthesis enables flexible manipulation of individual factors affecting the efficiency protein biosynthesis. However, the high cost and low stability of the energy sources to regenerate ATP have limited the use of cell-free synthesis for large-scale production of recombinant proteins. One of the approaches to address this problem is to use glucose as an alternative energy source to regenerate ATP through the glucose-metabolizing pathways in a cell extract. In this study, in an attempt to improve the efficiency of ATP regeneration by reinforcing oxidative phosphorylation process, we supplemented with cellular lipids to a glucose-fueled reaction mixture for cell-free protein synthesis. As a result of the lipid supplementation, the productivity of chloramphenicol acetyltransferase in a cell-free synthesis system using glucose increased more than 6 fold compared to when the lipid was not supplemented.