• 한국식품영양과학회:학술대회논문집
• /
• 한국식품영양과학회 2004년도 Annual Meeting and International Symposium
• /
• pp.80-84
• /
• 2004

• 한국당과학회:학술대회논문집
• /
• 한국당과학회 2006년도 제1회 연례학술대회
• /
• pp.63-63
• /
• 2006

• 한국당과학회:학술대회논문집
• /
• 한국당과학회 2006년도 제1회 연례학술대회
• /
• pp.64-64
• /
• 2006

• 대한약학회:학술대회논문집
• /
• 대한약학회 2001년도 Proceedings of the Pharmaceutical Society of Korea
• /
• pp.164.1-164.1
• /
• 2001

• 생약학회지
• /
• 제30권4호
• /
• pp.355-362
• /
• 1999

New lectins have been isolated and purified from mung bean (Phaseolus radiatus) through physiological saline extraction, ammonium sulfate salt fractionation and column chromatographies. Ion exchanger were eluted by linear salt gradient and then further purified through gel filtration. Thus obtained lectin named as MBL. The gene expressions of 5 cytokines (IL-1, IL-2, IL-6, $TNF-{\aphpa}$ and $IFN-{\gamma}$) from human peripheral blood mononuclear cells (PBMC) stimulated with MBL were investigated by using reverse transcription polymerase chain reaction (RT-PCR). PBMC ($1{\times}106$ cells/ml) isolated from healthy volunteers were stimulated with lectins (4 mg/ml) for various time intervals (1 to 96 hrs). After each of the various stimulated times, total RNA was isolated and assessed for different cytokines mRNA by RT-PCR. The mRNA encoding IL-1, IL-2 were detected continuously from 1 to 20 hrs, and IL-6 was detected up to 24 hrs. But the mRNA encoding $IFN-{\gamma}$ and $TNF-{\alpha}$ were detected to 8 hours only and showed short time response compared with other cytokines. The significant expression of all cytokines mRNA were observed at 4 hrs. These results suggested that MBL, as inducer of cytokines could elicit detectable cytokine mRNA from PBMC.

• BMB Reports
• /
• 제39권5호
• /
• pp.560-570
• /
• 2006

Mistletoe (Viscum album) lectins, which are classified as a type II ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the A-chain with catalytic activity and the B-chain with sugar binding properties. In recent years, studies involving the lectins from the white berry European mistletoe (Viscum album) and the yellow berry Korean mistletoe (Viscum album coloratum) have been described. However, the detailed mechanism in exerting unique cytotoxic effect on cancer cells still remains unclear. Here, we aim to understand and define the molecular basis and biological effects of the type II RIPs, through the studies of the recombinant Korean mistletoe lectin. To this end, we expressed, purified the recombinant Korean mistletoe lectin (rKML), and investigated its molecular characteristics in vitro, its cytotoxicity and ability to induce apoptotic cell death in cancer cells. To gain structural basis for its catalytic activity and sugar binding properties, we performed homology modeling studies based on the high degree of sequence identity and conserved secondary structure prediction between Korean and European, Himalayan mistletoe lectins, and Ricin.

• Journal of the Korean Wood Science and Technology
• /
• 제29권4호
• /
• pp.79-88
• /
• 2001

표고버섯(Lentinula edodes) 으로부터 0.15 M NaCl 용액에 의하여 crude lectin을 추출하였으며, 황산암모늄에 의한 침전 음이온교환수지 및 hydroxyapatite 컬럼을 이용한 크로마토그래피에 의하여 정제하였다. 버섯균산과 균병으로 나누어 추출된 crude lectin의 양에 있어서는 균산부분이 균병부분에 비하여 2배 이상 높은 lectin을 함유하였으며, 가열한 버섯에서는 lectin의 함량 및 활성은 미처리보다 감소되었다. 건조된 균산 50 g으로부터 얻은 crude lectin은 720 mg으로서 46.03%의 수율로 얻었으며, DEAE Sephadex A-50 column에 의한 분리, 정제 후 정제된 lectin 201 mg을 crude lectin의 28% 수율로 얻을 수 있었다. Crude lectin을 정제함으로서 aspartic acid, serine, alanine 및 histidine등의 아미노산이 증가되었고, glutamic acid, glycine, leucine, tyrosine 및 methionine 등이 lectin에는 검색되지 않았다. DEAE Sephadex A-50 column의 chromatograpy를 통해 분리 정제한 활성을 지니는 lectin의 주된 부분은 Agglutinating test 결과, fraction A 및 B는 적혈구응집활성을 나타냈으며, 약 23 kDa의 분자량을 가지고 있었다. 활성을 지니는 부분을 다시 hydroxyapatite column에 의해 정제하여 얻은 LA-a와 LB-b는 각각 24 kDa과 23 kDa의 분자량을 나타냈다.

• 한국식품과학회지
• /
• 제31권4호
• /
• pp.899-905
• /
• 1999

Aloe vera의 점액성의 젤리 및 녹색의 표피로부터 gel chromatography 및 친화크로마토그래피를 이용하여 렉틴을 분리하여 SDS-PAGE에 의하여 분자량을 확인하였다. 젤리로부터 분리된 물질을 전기영동한 결과, Sephadex G-100으로 정제한 경우, 58.7 kD와 33.3 kD의 분자량에서 band가 나타났고, 산처리한 Sepharose 4B column으로 정제한 렉틴의 경우에는 176.4 kD의 band가 나타났다. 표피로부터 분리된 물질을 전기영동한 결과, Sephadex G-100으로 정제한 경우, 221.1 kD, 54.0 kD, 32.5 kD에서 넓은 band가 나타났으며, 산처리 한 Sepharose 4B column으로 정제한 경우에는 222.0 kD 및 158.0 kD의 band가 나타났다. 산처리한 Sepharose 4B로부터 분리된 렉틴에 대한 당의 적혈구 응집력 억제효과를 측정한 결과, 젤리의 경우, D-galactose, lactose, D-galactosamine과 특이성이 있는 것으로 나타났으며, 그 중 lactose와 가장 큰 특이성이 있는 것으로 나타났다. 그러나, 표피의 경우에는 D-galactose, D-galactosamine에만 특이성이 있는 것으로 나타났으며, 젤리와는 달리 lactose와는 특이성이 없는 것으로 나타났다. 친화크로마토그래피로부터 분리된 렉틴에 대한 pH의 영향을 측정한 결과, 젤리와 표피로부터 얻은 시료 모두 pH $7.0{\sim}9.0$의 pH 범위에서 안정하였다. 또한, 온도의 영향을 측정한 결과, $0{\sim}60^{\circ}C$까지 100% 활성을 나타냈고 $70^{\circ}C$ 이상에서는 활성이 떨어지는 것으로 나타났다.

• 대한생식의학회:학술대회논문집
• /
• 대한불임학회 2002년도 제42차 춘계학술대회
• /
• pp.77-77
• /
• 2002

• BMB Reports
• /
• 제35권5호
• /
• pp.472-475
• /
• 2002

Phaseolus vulgaris phytohemagglutinin L is a homotetrameric-leucoagglutinating seed lectin. Its three-dimensional structure shows similarity with other members of the legume lectin family. The tetrameric form of this lectin is pH dependent. Gel filtration results showed that the protein exists in its dimeric state at pH 2.5 and as a tetramer at pH 7.2. Contrary to earlier reports on legume lectins that possess canonical dimers, thermal denaturation studies show that the refolding of phytohemagglutinin L at neutral pH is irreversible. Differential scanning calorimetry (DSC) was used to study the denaturation of this lectin as a function of pH that ranged from 2.0 to 3.0. The lectin was found to be extremely thermostable with a transition temperature around $82^{\circ}C$ and above $100^{\circ}C$ at pH 2.5 and 7.2, respectively. The ratio of calorimetric to vant Hoff enthalpy could not be calculated because of its irreversible-folding behavior. However, from the DSC data, it was discovered that the protein remains in its compact-folded state, even at pH 2.3, with the onset of denaturation occurring at $60^{\circ}C$.