• Title, Summary, Keyword: lectin

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Isolation and Characterization of Lectin in Soybean(Glycine max L.) (대두(Glycine max L.)의 렉틴 분리 및 특성)

  • 박원목;이용세;박상호;김성환;윤경은
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.34 no.2
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    • pp.120-126
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    • 1989
  • This experiment was carried out to investigate the lectin of soybean (Glycine max L.) seed. Purification was done by 50-80% ammonium sulfate precipitation, CM-cellulose and Sephadex G-100 column. The purity was ascertained by electrophoresis. The molecular weight of purified lectin was estimated as 132,000. It was composed of three subunits which molecular weight was 45,000. The lectin was identified as glycoprotein by Schiff's reagent staining and Dubois method. The lectin agglutinated erythrocytes of rabbit and human. The amounts of the lectin to agglutinate human erythrocytes differed among the blood types: The blood type A required the least amount, the next was B, O, and AB in order. The agglutination was specifically inhibited by 5${\mu}$g/ml of N -acetyl.-D-galactoseamine and 200${\mu}$g/ml of D-galactose. Other tested sugars could not inhibit the agglutination of the erythrocytes by the lectin.

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Effects of Supplementary Immune Modulators(MOS, Lectin) and Organic Acid Mixture(Organic acid F, Organic acid G) on the Performance, Profile of Leukocytes and Erythrocytes, Small Intestinal Microflora and Immune Response in Laying Hens (면역기능 조절제(MOS, Lectin)와 유기산제(Organic acid F, Organic acid G)가 산란계의 생산성, 혈액성상과 소장내 미생물 균총 및 면역체계에 미치는 영향)

  • Woo, K.C.;Kim, C.H.;Paik, I.K.
    • Journal of Animal Science and Technology
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    • v.49 no.4
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    • pp.481-490
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    • 2007
  • An experiment was conducted to investigate the effects of dietary supplementation of MOS, lectin and organic acid mixture(Organic acid F, Organic acid G) on the egg production, egg quality, profile of leukocytes and erythrocytes, small intestinal microflora and immune response in laying hens. A total of 900 Hy-line BrownⓇ laying hens of 48 wks old were assigned to one of the following 6 dietary treatments:control(C), C+AvillamycinⓇ 6ppm, C+MOS 250ppm, C+lectin 12.5ppm, C+Organic acid F(formic acid 35.4%, formate 34.6%, potassium 30.0%) 0.3% and C+0rgarnic acid G(fumaric acid 23%, calcium formate 14%, potassium sorbate 5%, calcium propionate 7%) 0.06%. Each treatment was replicated five times with thirty birds per replicate, housed in 2 bird cages. Feeding trial lasted for 6 wks under 16 hours lighting regimen. All supplemental groups were higher than the control in 6 wks hen-day and hen-housed egg production showing the highest with MOS treatment(P<0.05). Soft & broken egg productions were lower in supplemental groups than in the control except lectin treatment(P<0.05). Eggyolk color of supplemental groups was higher than that of the control except Organic acid G treatment(P<0.05). The values of RBC, HB, MCHC were highest in lectin treatment and lowest in MOS treatment(P<0.05). The numbers of intestinal microflora were not significantly different among the treatments. Serum IgG levels of all supplemental groups were higher than those of the control(P<0.05). In conclusion, for supplementation of antibiotics, immune modulators and organic acid mixture improved production parameters in general. Among the supplements, MOS showed the best performance in egg production and eggyolk color.

A Tuber Lectin from Arisaema jacquemontii Blume with Anti-insect and Anti-proliferative Properties

  • Kaur, Manpreet;Singh, Kuljinder;Rup, Pushpinder Jai;Kamboj, Sukhdev Singh;Saxena, Ajit Kumar;Sharma, Madhunika;Bhagat, Madhulika;Sood, Sarvesh Kumar;Singh, Jatinder
    • BMB Reports
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    • v.39 no.4
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    • pp.432-440
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    • 2006
  • A tuber lectin from Arisaema jacquemontii Blume belonging to family Araceae was purified by employing a single step affinity chromatography using column of asialofetuin-linked amino activated silica beads and the bound lectin was eluted with 100 mM glycine-HCl buffer pH 2.5. The purified A. jacquemontii lectin (AJL) showed a single protein band with an apparent molecular mass of 13.4 kDa when submitted to SDS-polyacrylamide gel electrophoresis under reducing as well as non-reducing conditions. The native molecular mass of AJL determined by gel filtration on a Biogel P-200 column was 52 kDa and its carbohydrate content was estimated to be 3.40%. Thus AJL is a tetrameric glycoprotein. The purified lectin agglutinated erythrocytes from rabbit but not from human. Its activity was not inhibited by any of the mono- and disaccharides tested except N-acetyl-D-lactosamine having minimal inhibitory sugar concentration (MIC) 25 mM. Among the glycoproteins tested only asialofetuin was found to be inhibitory (MIC $125\;{\mu}g/mL$). A single band was obtained in native PAGE at pH 4.5 while PAGE at pH 8.3 showed two bands. Isoelectric focusing of AJL gave multiple bands in the pI range of 4.6-5.5. When incorporated in artificial diet AJL significantly affected the development of Bactrocera cucurbitae (Coquillett) larvae indicating the possibility of using this lectin in a biotechnological strategy for insect management of cucurbits. Larvae fed on artificial diet containing sub-lethal dose of AJL showed a significant decrease in acid phosphatase and alkaline phosphatase activity while esterase activity markedly increased as compared to larvae fed on diet without lectin. Out of various human cancer cell lines employed in sulphorhodamine B (SRB) assay, this lectin was found to have appreciable inhibitory effect on the in vitro proliferation of HCT-15, HOP-62, SW-620, HT-29, IMR-32, SKOV-3, Colo-205, PC-3, HEP-2 and A-549 cancer cell lines by 82, 77, 73, 70, 41, 41, 37, 29, 21 and 21% respectively.

사료내 감태 및 감태로부터 추출한 crude lectin의 첨가가 육계의 생산성 및 면역반응에 미치는 영향

  • 김성권;유선종;안병기;박근규;이훈택;송창선;허억;강창원
    • Proceedings of the Korea Society of Poultry Science Conference
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    • pp.23-25
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    • 2004
  • This study was conducted to investigate the effects of dietary supplementation of Ecklonia cava kjellman(ECK) and crude lectin extracted from ECK (CLEEC) on performances and immune responses in broiler chicks. A total of two hundreds thirty four 1 day old male broiler chicks (Ross) were fed corn-soy based diets containing 0 % (with or without vaccination and Salmonella challenge), 1.0 % ECK, 0.05 %, 0.1 % and 0.3 % CLEEC for 38 days and vaccinated against inactivated ND-IB combined oil vaccine on the fourth day. After S. gallinarum challenge. mortality was measured daily. The spleens of birds were removed for RNA extraction and reverse transcription polymerase chain reaction (RT-PCR) with primer sets for IFN-ν, IL-2, IL-6 and ${\beta}$-actin were performed with RNA samples. At the 28th day, pancreas weights were heavier 0.3 % CLEEC than 1.0 % ECK group. At the 21st day after ND-IB oil vaccine injection, dietary supplementation of ECK and CLEEC tended to increase or significantly (P<0.05) improved ND or IB titer compared to the positive control. Mortality was significantly (P<0.05) decreased by dietary CLEEC treatments. Chicken splenic IFN-ν, IL-2, and IL-6 cytokines mRNA expressions were enhanced by challenge with S, gallinarum. Dietary treatments did not affect mRNA expression of IFN-ν. However, IL-2 and IL-6 expressions in Salmonella challenged birds that fed the 1.0 % ECK or 0.05 % CLEEC groups were enhanced (P<0.05) compare to the positive control. The results demonstrated that dietary ECK and CLEEC enhanced humoral and cellular immunity and therefore. it can be concluded that dietary supplementation of ECK and CLEEC can be used as a feed additive for enhancement of immunocompetence without any adverse effects in broiler chicks.

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Loss of Potential Biomarker Proteins Associated with Abundant Proteins during Abundant Protein Removal in Sample Pretreatment

  • Shin, Jihoon;Lee, Jinwook;Cho, Wonryeon
    • Mass Spectrometry Letters
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    • v.9 no.2
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    • pp.51-55
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    • 2018
  • Capture of non-glycoproteins during lectin affinity chromatography is frequently observed, although it would seem to be anomalous. In actuality, lectin affinity chromatography works at post-translational modification (PTM) sites on a glycoprotein which is not involved in protein-protein interactions (PPIs). In this study, serial affinity column set (SACS) using lectins followed by proteomics methods was used to identify PPI mechanisms of captured proteins in human plasma. MetaCore, STRING, Ingenuity Pathway Analysis (IPA), and IntAct were individually used to elucidate the interactions of the identified abundant proteins and to obtain the corresponding interaction maps. The abundant non-glycoproteins were captured with the binding to the selected glycoproteins. Therefore, depletion process in sample pretreatment for abundant protein removal should be considered with more caution because it may lose precious disease-related low abundant proteins through PPIs of the removed abundant proteins in human plasma during the depletion process in biomarker discovery. Glycoproteins bearing specific glycans are frequently associated with cancer and can be specifically isolated by lectin affinity chromatography. Therefore, SACS using Lycopersicon esculentum lectin (LEL) can also be used to study disease interactomes.

Thermal Stability of Phaseolus vulgaris Leucoagglutinin: a Differential Scanning Calorimetry Study

  • Biswas, Shyamasri;Kayastha, Arvind M.
    • BMB Reports
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    • v.35 no.5
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    • pp.472-475
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    • 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 $60^{\circ}C$.

Separation of Lentil Lectin Using Free-Flow Electrophoresis (자유유동 전기이동을 이용한 Lentil Lectin의 분리)

  • 류화원;이동일장호남
    • KSBB Journal
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    • v.9 no.2
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    • pp.115-121
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    • 1994
  • A Purification device with 30-channel free-flow electrophoresis was assembled to treat samples of 240m1 volume for purification of lentil lectin (LcH) from lentil seeds with no impurities in a silverstained PAGIEF gel. HEPES(50mM)-Ttis(50mM), Cycloserine(50mM)-urea(3M), Histidine(50mM)-urea(3M) were used as ampholytea among which Histidine(50mM)-urea(3M) (pI 7.65) was found best in resolution. LcH is known to be present in the form of LcH-A, LcH-B and the complex of the two. The complex, however, disappeared when urea was added in the ampholytes, which suggested that the complete purification of two isolectins is possible using the present multistep purificaton device.

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Molecular Characterization and Mitogenic Activity of a Lectin from Purse Crab Philyra Pisum

  • Na, Jong-Cheon;Park, Byung-Tae;Chung, Woo-Hyuk;Kim, Ha-Hyung
    • The Korean Journal of Physiology and Pharmacology
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    • v.15 no.4
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    • pp.241-244
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    • 2011
  • A lectin from the hemolymph of purse crab, Philyra pisum, was found to have anti-proliferative activity on human lung cancer cells by our laboratory. In this study, P. pisum lectin (PPL) was molecularly characterized including molecular mass, amino acid sequences, amino acid composition, and the effects of metal ions, temperature, and pH on the activity. We found that PPL showed mitogenic activity on human lymphocytes and BALB/c mouse splenocytes. The mitogenic activity (maximum stimulation index, $SI=9.57{\pm}0.59$) of PPL on human lymphocytes was higher than that of a standard well-known plant mitogen, concanavalin A (maximum $SI=8.80{\pm}0.59$). The mitogenic activity mediated by PPL is required for optimum dosing, and higher or lower concentrations caused decreases in mitogenic response. PPL also induced mitogenic activity on mouse splenocytes, however, the maximum SI ($1.77{\pm}0.09$) on mouse splenocytes of PPL was lower than that ($2.14{\pm}0.15$) of concanavalin A. In conclusion, PPL is a metal ion-dependent monomer lectin with mitogenic activity, and could be used as a lymphocyte or splenocyte stimulator.

The Rapid Differentiation of Toxic Alexandrium and Pseudo-nitzschia Species Using Fluorescent Lectin Probes

  • Cho, Eun-Seob;Park, Jong-Gyu;Kim, Hak-Gyoon;Kim, Chang-Hoon;Rhodes, Lesley L.;Chung, Chang-Soo
    • Journal of the korean society of oceanography
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    • v.34 no.3
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    • pp.167-171
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    • 1999
  • Since toxic Alexandrium catenella and non-toxic A. fraterculus are morphologically similar, they are difficult to discriminate under the light microscope. However, a novel technology, such as fluorescein isothiocyanate (FITC)-conjugated lectin probes enables easy and rapid differentiation. Toxic A. catenella bound seven different lectins, whereas the non-toxic A. fratercuzus did not bind Arachis hypogaea (PNA) lectin. In addition, Pseudo-nitrschia species in this study were also difficult to identify to species level with light microscope techniques, but it was possible to classify them using fluorescent lectins. Pseudo-nitzschia multistriata, P. subfraudulenta and P. pungens bound Canavalia ensiformis (ConA), whereas P. subpaclfica did not, and P. pungens also bound Ricinus communis (RCA). These results imply that lectin could be used as a critical tool in the differentiation of P. multistriata, P. subfraudulenta and P. pungens. However, P. subpacifica was not differentiated by the lectins tested. Therefore, it isconcluded that lectin probes are useful for discriminating toxic A. catenella from non-toxic A. fraterculus, and for the identification of some Pseudo-nitzschia species. In addition, this method has a great potential to speed and detection between non-toxic and toxic harmful algal blooms (HABs) in Korean biotoxin monitoring systems.

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돼지의 체외수정시 투명대내 Lectin 결합과 수정촉진 Peptide의 영향

  • 황인선;정희태;양부근;김정익;박춘근
    • Proceedings of the KSAR Conference
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    • pp.13-13
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    • 2002
  • 수정촉진 peptide(Fertilization Promoting Peptide; FPP) 는 체내에서 정자-난자의 결합시 투명 대내에서 glycoprotein 과 progesterone에 의해 정자침입이 활성화 될 때까지 첨체반응을 억제함으로써 정자의 수정상태 유지를 위하여 필요한 물질로 알려져 있다. 한편, 정자내에 존재하는 lectin과 같은 단백질 및 효소 등은 투명대내에 존재하는 oligosaccharide 잔기를 합성시킨다. 본 연구는 돼지 정자-난자의 체외수정시 투명대내 FITC-labelled 처리된 lection의 결합과 FP의 영향을 검토하고자 수행되었다. (중략)

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