• 한국미생물·생명공학회지
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• 제36권2호
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• pp.128-134
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• 2008

Erro-prone PCR에 의해서 열안정성이 향상된 Streptomyces coelicolor A(3) 유래의 L-threonine aldolase를 Corynebacterium glutamicum R에서 과잉발현시키기 위하여 Corynebacterium용 vector plasmid인 pCRB1의 SD배열과 개시코든사이의 1염기를 제거한 고발현용 vector plasmid인 pCG-H44(2)를 구축하였다. pCG-H (2)에 의해서 형질전환된 C. glutamicum R 균주(CGH44-2)에서 L-TA를 발현시킨 결과, 기존의 Corynebacterium용 vector plasmid인 pCRB1(CGH44-1)보다 L-TA의 발현량이 높았다. L-threo-DOPS의 합성을 위한 최적조건은 $30^{\circ}C$, 0.1 M cirtric acid buffer(pH 7.0)이었으며, 0.1% TritonX-100를 첨가하였을 경우 보다 높은 활성을 보였다. 최적조건하에서 CGH44-2를 whole cell biocatalyst로 이용한 반복회분식반응에서 재조합대장균을 숙주로 이용한 경우보다 재조합Corynebacterium을 이용하였을 경우, 목적하는 L-threo-DOPS의 합성이 안정적으로 이루어졌다.

• Journal of Plant Biotechnology
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• 제30권4호
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• pp.323-328
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• 2003

토양 내의 고농도의 염은 심각한 환경스트레스 중의 하나로 농작물의 생산을 감소시킨다. 식물은 염 스트레스로부터 벗어나기 위하여 많은 단백질을 합성한다든지 유전자들의 발현을 조절하는 등 여러 가지 생리, 생화학적인 변화를 일으킨다. 퉁퉁마디는 우리나라에 자생하는 염생식물로 갯벌과 염전주위에서 생육한다. 퉁퉁마디의 생화학적, 분자생물학적 내염성 기구를 이해하기 위하여 differential display방법으로 NaCl에 의하여 발현이 증가되는 cDNA들을 분리하였다. 본 연구에서는 그 중 하나인 ShADL의 특성을 조사하였다. ShADL은fructose-1, 6-bisphosphate aldolase와 높은 유사성을 보였다. 이 유전자는 1293bp길이에 359개의 아미노산으로 구성된 open reading frame을 포함하고 있으며, 이로부터 추정되는 분자량은 39 kDa이었다. ShADL단백질은 애기장대의 aldolase와 86％의 높은 유사성을 나타내었으며 같은 염생식물인 com-mon ice plant의 adolase와는 78％의 유사성을 보였다. Northern 분석결과, ShADL 유전자는 NaCl의 농도가 증가함에 따라 발현량이 급격히 증가하는 것으로 나타났다.

• 대한한방내과학회지
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• 제17권1호
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• pp.51-65
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• 1996

This experimental study was designed to investigate the effects of Cibotii Rhizoma on the muscle atrophy induced by hindlimb suspension in rats. The measurement has been performed on the activity of CK, aldolase, LDH, AST, ALT and quantity of creatine in serum of hindlimb suspension rats. The results were as ; 1. Cibotii Rhizoma significantly inhibited the increase of the activity of CK in serum. 2. Cibotii Rhizoma significantly inhibited the increase of the quantity of creatine in serum. 3. Cibotii Rhizoma significantly inhibited the increase of the activity of aldolase in serum. 4. Cibotii Rhizoma significantly inhibited the increase of the activity of LDH in serum. 5. Cibotii Rhizoma significantly inhibited the increase of the activity of AST in serum. 6. Cibotii Rhizoma significantly inhibited the increase of the activity of ALT in serum.

• BMB Reports
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• 제49권12호
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• pp.681-686
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• 2016

Fructose 1,6-bisphosphate aldolase (FBA) is important for both glycolysis and gluconeogenesis in life. Class II (zinc dependent) FBA is an attractive target for the development of antibiotics against protozoa, bacteria, and fungi, and is also widely used to produce various high-value stereoisomers in the chemical and pharmaceutical industry. In this study, the crystal structures of class II Escherichia coli FBA (EcFBA) were determined from four different crystals, with resolutions between $1.8{\AA}$ and $2.0{\AA}$. Native EcFBA structures showed two separate sites of Zn1 (interior position) and Zn2 (active site surface position) for $Zn^{2+}$ ion. Citrate and TRIS bound EcFBA structures showed $Zn^{2+}$ position exclusively at Zn2. Crystallographic snapshots of EcFBA structures with and without ligand binding proposed the rationale of metal shift at the active site, which might be a hidden mechanism to keep the trace metal cofactor $Zn^{2+}$ within EcFBA without losing it.

• Journal of Microbiology and Biotechnology
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• 제20권6호
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• pp.995-1000
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• 2010

A novel deoC gene was identified from Paenibacillus sp. EA001 isolated from soil. The gene had an open reading frame (ORF) of 663 base pairs encoding a protein of 220 amino acids with a molecular mass of 24.5 kDa. The amino acid sequence was 79% identical to that of deoxyribose 5-phosphate aldolase (DERA) from Geobacillus sp. Y412MC10. The deoC gene encoding DERA was cloned into an expression vector and the protein was expressed in Escherichia coli. The recombinant DERA was purified using Ni-NTA affinity chromatography and then characterized. The optimum temperature and pH of the enzyme were $50^{\circ}C$ and 6.0, respectively. The specific activity for the substrate deoxyribose 5-phosphate (DR5P) was $62\;{\mu}mol/min/mg$. The $K_m$ value for DR5P was determined to be 145 mM with the $k_{cat}$ value of $3.2{\times}10^2/s$ from Lineweaver-Burk plots. The EA001 DERA showed stability toward a high concentration of acetaldehyde (100 mM).

• Parasites, Hosts and Diseases
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• 제51권2호
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• pp.155-163
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• 2013

This study aimed to evaluate the efficacy of fructose-1,6-bis phosphate aldolase (SMALDO) DNA vaccination against Schistosoma mansoni infection using different routes of injection. The SMALDO has been cloned into the eukaryotic expression vector pcDNA3.1/V5-His TOPO-TA and was used in injecting Swiss albino mice intramuscularly (IM), subcutaneously (SC), or intraperitoneally (IP) ($50{\mu}g/mouse$). Mice vaccinated with non-recombinant pcDNA3.1 served as controls. Each group was immunized 4 times at weeks 0, 2, 4, and 6. Two weeks after the last booster dose, all mice groups were infected with 80 S. mansoni cercariae via tail immersion. At week 8 post-infection, animals were sacrificed for assessment of parasitological and histopathological parameters. High anti-SMALDO IgG antibody titers were detected in sera of all vaccinated groups (P<0.01) compared to the control group. Both the IP and SC vaccination routes resulted in a significant reduction in worm burden (46.2% and 28.9%, respectively, P<0.01). This was accompanied by a significant reduction in hepatic and intestinal egg counts (41.7% and 40.2%, respectively, P<0.01) in the IP group only. The number of dead eggs was significantly increased in both IP and IM groups (P<0.01). IP vaccination recorded the highest significant reduction in granuloma number and diameter (54.7% and 29.2%, respectively, P<0.01) and significant increase in dead miracidia (P<0.01). In conclusion, changing the injection route of SMALDO DNA vaccination significantly influenced the efficacy of vaccination. SMALDO DNA vaccination via IP route could be a promising protective and antipathology vaccine candidate against S. mansoni infection.

• Molecules and Cells
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• 제28권6호
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• pp.559-563
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• 2009

Glyceraldehyde-3-phosphate is a key intermediate in several central metabolic pathways of all organisms. Aldolase and glyceraldehyde-3-phosphate dehydrogenase are involved in the production or elimination of glyceraldehyde-3-phosphate during glycolysis or gluconeogenesis, and are differentially expressed under various physiological conditions, including cancer, hypoxia, and apoptosis. In this study, we examine the effects of glyceraldehyde-3-phosphate on cell survival and apoptosis. Overexpression of aldolase protected cells against apoptosis, and addition of glyceraldehyde-3-phosphate to cells delayed apoptosis. Additionally, delayed apoptotic phenomena were observed when glyceraldehyde-3-phosphate was added to a cell-free system, in which artificial apoptotic process was induced by adding dATP and cytochrome c. Surprisingly, glyceraldehyde-3-phosphate directly suppressed caspase-3 activity in a reversible noncompetitive mode, preventing caspase-dependent proteolysis. Based on these results, we suggest that glyceraldehyde-3-phosphate, a key molecule in several central metabolic pathways, functions as a molecule switch between cell survival and apoptosis.

• 한국식품영양학회지
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• 제10권1호
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• pp.65-73
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• 1997

본 실험은 벌꿀이 흰쥐(Sprague Dawley, ♂)의 효소활성에 미치는 영향을 구명하고저 설탕, 아카시아, 붉나무 그리고 잡화벌꿀을 각각 10%와 20%의 수용액으로 만들어 7주간 섭취 한 후 벌꿀의 효과를 비교한 바 다음과 같은 결론을 얻었다. LDH활성은 대조군에 비하여 아카시아꿀, 붉나무꿀, 잡화꿀용액 섭취군에서 증가하였다. $\alpha$-HBDH활성은 설탕용액, 아카시아꿀, 붉나무꿀, 잡화꿀용액 섭취군이 대조군에 비하여 증가하였다. 벌꿀 섭취군 중 20% 아카시아꿀 용액만 GOT, GPT의 활성이 증가하였다. ICD활성은 붉나무꿀 용액에서 증가하였으나 아카시아 및 잡화꿀 용액에서 뚜렷하게 감소되었다. 벌꿀용액 섭취는 PHI, 전혈 G-6-P DH 활성을 감소시켰으나, aldolase역가를 증가시키는 경향이었다.

• 미생물학회지
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• 제8권1호
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• pp.35-40
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• 1970

In the cell-free systems of Dunaliella tertiolecta, fructosediphosphate aldolase hardly contribute to synthesize hexosephosphate from triosephosphate derived from pentosphosphate pathway, and it could be considered that glycerol synthesized from added glucose was synthesized but via 3-phosphoglyceraldehyde as an intermediate not hydroxypyruvate.

• 한국식품과학회지
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• 제31권1호
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• pp.62-67
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• 1999

과요오드산 산화 가용성전분 및 말토올리고당을 고구마 ${\beta}-amylase$, 밀 ${\beta}-amylase$, aldolase, bovine serum albumin, catalase, carboxypeptidase, ferritin, pronase와 반응시켜서 전기영동하였다. 이들 단백질은 전기영동상의 이동도가 달라지고, 단백질 밴드와 같은 위치에서 PAS 염색 밴드를 나타내어 당이 부가된 것으로 확인되었다. 당의 부가는 과요오드산 산화당의 알데히드기가 단백질 분자 표면 리신의 ${\varepsilon}-NH_2$기와 Schiff 염기를 형성하여 일어난다. 변형효소는 자외흡광곡선에 변화를 나타내지 않았다.