• Title, Summary, Keyword: Lectin

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Characterization of the Lectin Purified from Canavalia ensiformis Shoots

  • Roh, Kwang-Soo;Park, Na-Young
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.10 no.4
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    • pp.334-340
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    • 2005
  • Lectin is a cell-agglutinating and carbohydrate-binding protein present in many plants. The lectin of Canavalia ensiformis shoot with specific affinity for D-glucose was purified by affinity chromatography using Sephadex G-100, and some of its biochemical characterizations were studied. Lectin was purified 8.87-fold and exhibited final specific activity of 225.74 units/mg protein with a $2.3\%$ yield. SDS-PAGE analysis demonstrated that the purified shoot lectin exists as a tetramer of 102 kD, composed of two subunits with molecular weight of 29 and 22 kD. The purified lectin was observed to agglutinate rabbit blood cell. The optimal temperature for the activity of this lectin was $40^{\circ}C$, and this lectin was relatively stable to heat with the highest activity at $50{\~}60^{\circ}C$. The maximal activity was observed at pH 7.2.

Toxicity of lectin extracted from Korean mistletoe (Viscum album coloratum) in chicks and its immunoadjuvant activity on Newcastle disease virus vaccines (한국산 겨우살이(Viscum album coloratum)로부터 추출된 lectin의 닭에 대한 독성 및 뉴캐슬병 백신의 특이면역 증강 효과)

  • Yeo, Sang-Geon
    • Korean Journal of Veterinary Research
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    • v.46 no.3
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    • pp.215-224
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    • 2006
  • In order to search the availability of the lectin extracted from Korean mistletoe(Viscum album coloratum) as an adjuvant for the avian vaccines, attempts were made to determine toxicity of the lectin in chicks and its immunostimulating activity on the inactivated vaccines against Newcastle disease virus(NDV). For the determination of toxicity, the lectin was injected into the thigh muscle of SPF chicks(Charles River) of 1-week-old and observed hematologically and pathologically. For the determination of immunostimulating effects, lectin-adjuvanted, inactivated NDV vaccines were injected into the thigh muscle of SPF chicks in the same age group. Sera of the chicks were examined for the hemagglutination-inhibition(HI) antibodies induced, their HI titers and reaction to the NDV antigens. The data were further compared with those from aluminum hydroxide [$Al(OH)_3$]-adjuvanted vaccines and vaccines without adjuvant, and the results are as follows. There were no significant changes observed in the values of RBC, WBC, Hb, PCV, MCV, MCH, MCHC, AST, ALT, BUN, creatinine and total proteins in the chicks administered with lectin of 1.1, 2.2 and $22.2{\mu}g/kg$ body weight, which means the lectin has no effects on blood values and functions of liver and kidney. In histopathologic observation, no lesions were observed in the brain, heart, liver, lung, spleen, kidney, thymus and bursa of Fabricius of the chicks administered with lectin of 1.1, 2.2 and $22.2{\mu}g/kg$ body weight. There were inflammatory lesions, such as congestion, hemorrhage, edema, infiltration of macrophages and coagulation necrosis observed in the thigh muscle of chicks administered with lectin of $22.2{\mu}g/kg$ body weight, whereas no changes were observed in 1.1 and $22.2{\mu}g/kg$ lectin administered chicks. In chicks immunized with lectin($4.4{\mu}g/kg$ of body weight)-adjuvanted B1, LaSota and Ulster 2C vaccines, HI titers in reciprocal values for $log_2$ were 1.8-2.2 at 1 week after vaccination, which was similar with those of 1.5-2.9 by $Al(OH)_3$-adjuvanted vaccines. The HI titers by the lectin-adjuvanted vaccines reached to 3.9-5.3 at 4 weeks, whereas those by the $Al(OH)_3$-adjuvanted vaccines were more high as 7.3-9.3. Meanwhile, the immunostimulating effects of the lectin were recognized while compared to the HI titers with 2.4-3.7 in chicks immunized with vaccines without adjuvants at 4 weeks after vaccination. The chicks immunized with lectin-adjuvanted vaccines were enough to resist challenges by Kyojeongwon strain, a very virulent NDV at 4 weeks after vaccination as well as chicks immunized with $Al(OH)_3$-adjuvanted vaccines. The HI titers by the lectin-adjuvanted vaccines reached to high level as 8.7-10.3 as those with 8.2-9.6 by the $Al(OH)_3$-adjuvanted vaccines at 6 weeks after vaccination, which may be the booster effects by the challenge virus. Antibodies specific to the HN and F antigens of NDV were observed in the sera of both chicks immunized with lectin-adjuvanted vaccines and $Al(OH)_3$-adjuvanted vaccines.

Purification and Biochemical Characterization of Lectin from Viscum album (겨우살이 Lectin의 정제 및 생화학적 특성)

  • Jang, Cheol-Su;O, Mi-Jeong;No, Gwang-Su
    • KSBB Journal
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    • v.14 no.5
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    • pp.578-584
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    • 1999
  • The lectin was purified through 0.15 M NaCl extraction, ammonium sulfate precipitation, sepharose 4B affinity chromatography and gel filtration using sephadex G-150 from the leaves of Visum album collected in Mt. Duk Yu. The final gel filtration step resulted in 11.64 folds purification with 0.14% of recovery yield. We also performed biochemical characterization of the purified Visum album lectin. HPLC analysis of lectin purified by gel filtration revealed a singel peak. The analysis of the purified lectin by SDS-PAGE showed a tetramer composed of two identical subunits with molecular weights of 32 and 30 kDa. The lectin was a glycoprotein containing 14.4% carbohydrate, which consist of glucose, fructose, arabinose and xylose, and the amino acids such as phenylalanine, lysine and tyrosine. The purified lectin agglutinated human red blood cell types with similar potency, but when tested against red blood cells from mouse, bovine, rabbit, chicken and porcine, significant difference in potency were observed. Hemaggluting activity was inhibited by D-galactose, D-mannose, D-lactose and D-raffinose, but not by D-glucose, D-glucosamine, D-mannosamine, L-fructose, D-xylose, D-arabinose, D-galacturonic acid, D-fructose, L-rhamnose and N-acetyl-D-galactosamine. The optimal pH and thermal stability of the purified lectin were pH 4.0-7.0 and 20-5$0^{\circ}C$, respectively.

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Binding between Lipopolysaccharide of Rhizobia and Lectins from Soybean (대두 근류균의 리포 다당과 Lectin의 결합성)

  • Kang, Sang-Jae;Kim, Jin-Ho;Park, Woo-Churl
    • Current Research on Agriculture and Life Sciences
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    • v.15
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    • pp.25-32
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    • 1997
  • This study was carried out to research the biological characteristics among rhizobia and soybean seed and root lectins, and to obtain a basic imformation of host specificity in biological nitrogen symbiosis system. The results obtained were as follows: Purified seed lectin from soybean varieties of paldal, backwoon and hwangkeum formed immunoprecipitin lines with standard soybean seed lectin and the root lectins from soybean seedlings immunoelectrophoretically. Soybean seed and root lectins interacted with Rhizobium japonicum and Bradyrhizobium japonicum, but didn't interacted with Rhizobium. viceae, whereas pea lectin conjugated with R. viceae, but didn't bind with R. japonicum and B. japonicum. Lipopolysaccharides of B. japonicum and R. viceae were fractionated into LPS I and LPS II on the sephadox G-50. Lipopolysaccharides from B. japonicum showed rhe binding acitivity both with soybean seed lectin and root lectin, but those from R. viceae didn't show it with soybean seed and root lectins.

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Biochemical Properties of Eggplant Fruit Lectin. (가지 열매 lectin의 생화학적 성질)

  • Roh, Kwang-Soo
    • Journal of Life Science
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    • v.18 no.3
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    • pp.350-356
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    • 2008
  • Biochemical characterization including hemagglutination of erythrocytes, molecular weight, optimum temperature, thermal stability, optimum pH, carbohydrate specificity, and inhibitory effect of metal ion were studied in lectin of eggplant (Solanum melongena L.) fruit prepared by ammonium sulfate fractionation and affinity chromatography. This lectin was agglutinated by trypsin-treated rat blood erythrocyte. The molecular weight of this lectin by SDS-PAGE was estimated to be approximately 19.3 kDa of a single band. This lectin has no activity by 7 carbohydrates containing D-glucose. The optimum range of temperature and pH were $10-20^{\circ}C$ and pH 6.2-7.2, respectively. This lectin was relatively stable at $20-70^{\circ}C$. And the activity of this lectin was not inhibited by $Ca^{2+},\;Co^{2+},\;Cu^{2+},\;Fe^{2+},\;Mg^{2+}$, and $Mn^{2+}$.

Biochemical Characterization of Lectin Isolated from Cherry Tomato Fruit (방울토마토 열매로부터 분리된 lectin의 생화학적 특성)

  • Park, Na-Young;Lee, Sam-Pin;Roh, Kwang-Soo
    • Journal of Life Science
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    • v.17 no.2
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    • pp.254-259
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    • 2007
  • Biochemical characterization of lectin isolated from fruit of cherry tomato through neutral saline extraction, ammonium sulfate precipitation, and affinity chromatography on Sephadex G-200 was studied. The lectin was agglutinated by trypsin-treated human ABO erythrocytes, and the most pronounced activity of agglutination was observed at B type erythrocyte. The analysis of the lectin by SDS-PAGE showed the high intensity band with molecular weights of 10.7 kDa. The optimal temperature and thermal stability of the lectin was $40^{\circ}C$ and $40-60^{\circ}C$, respectively. The maximal pH of this lectin was pH 7.2.

Comparison of Biochemical Characterization of Korean and Chinese Mung Bean Lectin (한국산 녹두와 중국산 녹두에 있어서 Lectin의 생화학적 특성 비교)

  • Roh, Kwang Soo
    • Journal of Life Science
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    • v.24 no.6
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    • pp.603-611
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    • 2014
  • The lectins were separated from Korean and Chinese mung bean seeds finally via chromatography using Sephadex G-100 and their biochemical features were studied and compared. They showed no hemagglutination with human red blood cells regardless of trypsin treatment and showed hemagglutination with only trypsin treated rabbit red blood cells. The molecular weights of two lectins were identified as 54 kDa and 28 kDa by SDS-PAGE. It was found that while the optimal reaction temperature of the lectin from Korean mung bean was $60^{\circ}C$, that of the lectin from Chinese mung bean seeds was $50^{\circ}C$. It was found also that the most thermal stable temperature of the seed lectin from Korean mung bean seeds was $50^{\circ}C$ and the lectin from Chinese mung bean was $40-50^{\circ}C$. The lectin from Korean mung bean seeds showed the highest activity at pH 3.2 and the lectin from Chinese mung bean showed the highest activity at pH 6.2. It was identified that when treating a denaturant, thiourea and guanidine-HCl resulted in no hemagglutination, so they induced denaturalization. It was identified also that there was no hemagglutination with urea, so it did not induced denaturalization. They showed no septicity to 6 types of carbohydrates including D-glucose. In addition, the lectins from the two mung bean seed had specificity to metal ions.

The Comparative Studies on the Lectins from Kintoki Bean and Taro Tuber (팥콩 Lectin과 토란 Lectin의 특성 비교)

  • Young-Ju Seo
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.23 no.3
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    • pp.515-519
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    • 1994
  • The ComparativThe comperisons of Kintoki bean lectin (KBL) and Taro tuber lectin (TTL) which have been studied in our laboratory are summerized. The recoveries of pure lectins are 0.12% and 0.014%, respectively. They seems to have slight differences in isoelectric points(pH) ; 5.19~5.67 for KBL and 6.41~7.42 for TTL. The minimum concentrations of HA are $2.8\mu\textrm{g}/ml\;and\;21.6\mu\textrm{g}/ml$. The enzymatic modification on HA, growth inhibition, inhibition of nutritional absorption and binding capacities (FITC, $^3H$) of KBL are demonstrated to be much greater than those of TTL.

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Changes of Lectin from Viscum coloratum by Fermentation with Lactobacillus plantarum : Effect of pH and Temperature, Suger Specificity and Lymphocyte Stimulting Activity (유산균 발효에 의한 겨우사리 중의 렉틴 성분의 변화 : pH, 온도의 영향, 당 특이성, 림프구 자극분열효과)

  • 박원봉;김희숙;나혜복;함승시
    • YAKHAK HOEJI
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    • v.39 no.1
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    • pp.24-30
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    • 1995
  • Lectin from mistletoe(Viscum coloratum) fermented by Lactobacillus plantarum was compared with the lectin from unfermented mistletoe. Agglunating activity of fermented mistletoe was stable at pH 3.77~8.71, at temperature range of $0~40^{\circ}C$ and in the presence of 9 mental ions, which results are similar to unfermented one, but less stable at pH 2.03~3.00 and more stable at temperature $60~80^{\circ}C$ than lectin from unfermented one. Agglunating activity of lectin from mistletoe fermented for 1 or 2 days and from fraction number 42~54 was not inhibited by all sugars used except for lectin from fraction number 21~34. Mitogenic activity to murine lymphpocytes of lectin from mistletoe was decreased by fermentation process.

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Biochemical Properties of Seed Lectin from Korean Soybean Cultivars Developed for Soy Source (한국산 장류콩 종자 렉틴의 생화학적 특성)

  • Wang, Yushan;Roh, Kwang-Soo
    • KSBB Journal
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    • v.24 no.2
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    • pp.170-176
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    • 2009
  • Lectin was finally isolated on Sephadex G-100 from Korean soybean cultivars developed for soy source and investigated its some biochemical properties. Native PAGE pattern of this lectin revealed a molecular weight of 108 kDa as tetramer. The molecular weight of this lectin isolated as double protein band by SDS-PAGE was calculated to be 32 and 22 kDa from the relative mobilities compared with those of the standard proteins. Among the tested red blood cell, the isolated lectin agglutinated rabbit red blood cell treated with trypsin, but did not agglutinated human red blood cells (A, B, AB, O), rat, and untreated rabbit red blood cell. The optimal temperature and thermal stability of isolated lectin was at 20-$50^{\circ}C$ and 10-$60^{\circ}C$, respectively. This lectin was stable at 7.2, and showed complete loss in its activity below pH 6.2 and above pH 8.0.