1.Purification and preliminary studies for application of lectin from haemolymph clam (Meretrix meretrix Linne) in medicine.
Journal of Medical and Pharmaceutical Information 1998;(1):34-38
A lectin from the haemolymph clam was purified by molecular sieving on sephadex- G75 column. The products have a high purity. The purity of lectin was assessed by SDS polyacrylamide gel. Two doublets band of apparent molecular weights of respectively about 14,000-17,000 and 20,000-23,000 Dalton were revealed upon staining with Coomassie blue. Optimum-pH of the lectin from the clams is pH 6,5-7,0 and 8,5-9,0. The lectins of the clams had very different specificity for hydratecarbons and glucoproteins
isolation & purification
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Lectins
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medicine
2.Purification of Lectin (Abrus precatorius) and its application in detecting pathogenic bacteria
Journal of Preventive Medicine 2005;15(5):112-116
Lectin (APA) was purified from jequirity bean (Abrus precatorius) by affinity chromatography on insoluble ovomucoid. Lectin (APA) and conjugate Lectin-biotin have been used in ELLA technique (Enzyme Linked Lectinosorbent Assay) to detect some pathogenic bacteria. Based on its specific bioavailability to the poD-Gal sugar compounds in cell membrane, lectin (APA) was capable of differentiating B. anthracis and B. cereus from S. flexneri, S. sonnei, C. diphteria, and Salmonella and Staphylococcus aureus.
Lectins
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Abrus
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Diagnosis
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Bacteria
3.Experiment on using lectin extracted from seeds of abrus precatorius in identifying some viruses
Journal of Practical Medicine 2005;517(8):3-4
A study was conducted on biological active element lactin and clean lactin-biotin from Abrus precatorius in Hung Yen province. Result: clean lactin production from abrus precatorius and combination of Lectin (APA)-biotin were used to make ELISA to realize some disease-caused bacteria. Clean lectin (APA) related specific with original sugar β- D- Gal so it is able to realize B. anthracis bacterium and B. Cereus. Lectin (APA) does not connect with S. flexneri, S. sonnei, C.diphteriae and Salmonella bacteria. The findings of trial bring the new research approach in applying lectin in immunology production to contribute in diagnosis accurately bacterium strain cause disease.
Viruses
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Lectins
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Abrus
4.The value of AFP with lectins affinity in the diagnosis, distinguishable diagnosis, and observation the effects of treatment hepatocellular carcinoma
Journal of Practical Medicine 2005;515(7):71-74
Examination the usefulness of the lectin reactive alpha-fetoprotein (AFP-L3) in patients with hepatocellular carcinoma (HCC), chronic liver disease (CLD) and patients with HCC treated by transcatheter oil chemoembolization (TOCE). AFP-L3 levels were measured by lectins affinity electrophoresis and antibody affinity blotting. After TOCE, 40 HCC patients were divided in two groups: 1st group (n=27) with AFP-L3 < 15%; 2nd group (n=13) with AFP-L3 > 15%. Results: The mean value of AFP-L3 in the 110 HCC patients was 54.6 23.7%, significantly higher (p<0.001) than the value in CLD (11.2 3.1%). When the cut-off level was set 15% for AFP-L3, the sensitivity was 96.4%, the specificity was 95%. Survival rates after 12 and 18 months for all 27 patients calculated according to the Kaplan-Meier methods were 88.9% and 63% in the 1st group and 38.5% and 15.3% in the 2nd group, respectively. The recurrence of HCC for 1st and 2nd group were 10.2 3.5 months and 12.0 1.7 months, respectively.
Carcinoma, Hepatocellular
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Diagnosis
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Lectins
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alpha-Fetoproteins
5.Purification and identification of some characteristics of lectin from stament of Lotus (Nelumbo nucifera) and flowers of Telosma cordata
Pharmaceutical Journal 2001;298(2):15-18
The Lectin from Nulumbo nucifera and Telosma cordata have been extracted and purified by following process: Extraction with suitable medium precipitation with Ammoniumsunphate or Ethanol - ion exchange chromatography on CM-Cellulose of DEAE-Cellulose. Preparations having high purity showed homogeneous proteins in SDS-polyacrylamide gel-electrophoresis. pH-Optimum of the lectins from Nelumbo nucifera is pH 8.3, but form Telosma cordata is pH 5.5. The potency order of agglutination with monosaccharides was as Fructose, NAc-Glucosamine, Arabinose and NAc-acid Neuraminic for Nelumbo nucifera, but the lectin from Telosma cordata was inhibited only by Fructose, Saccharose NAc acid neuraminic. The lectins from Nelumbo nucifera and Telosma cordata were inhibited by many proteins from original Animals
Lectins
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Lotus
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Plants, Medicinal
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Medicine, Traditional
6.Histochemical study of lectin-binding patterns in the rat vomeronasal organ during postnatal development.
Wonho LEE ; Meejung AHN ; Changnam PARK ; Kazumi TANIGUCHI ; Changjong MOON ; Taekyun SHIN
Korean Journal of Veterinary Research 2012;52(1):1-8
Histochemical patterns of lectin binding during development of the rat vomeronasal organ (VNO) were studied to determine whether glycoconjugates are differently expressed after birth. Three types of lectins, Dolichos biflorus agglutinin (DBA), wheat germ agglutinin (WGA), and Ulex europaeus agglutinin I (UEA-I), were studied histochemically in the rat VNO at various stages post-birth: postnatal days 1 and 7, the preweaning period (4 weeks after birth), and at sexual maturity (8 weeks after birth). The free border of the vomeronasal sensory epithelium was positive for both WGA and UEA-I in rats of all ages; whereas, VNO receptor cells and supporting cells were positive only for both WGA and UEA-I from 4 weeks after birth. DBA reactivity was detected in the free border but less so in receptor cells and supporting cells. WGA and UEA-I, but not DBA, showed similar patterns in various ages. In the Jacobson's gland, WGA, UEA-I and DBA were detected in some acini from 4 weeks after birth but not at postnatal days 1 or 7. Collectively, reactivity for three lectins, WGA, UEA-I and DBA, increased in receptor cells and gland acini during postnatal development, possibly contributing to the enhanced chemoreception in rats.
Animals
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Dolichos
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Epithelium
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Glycoconjugates
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Lectins
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Parturition
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Plant Lectins
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Rats
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Triticum
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Ulex
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Vomeronasal Organ
7.Lectins in Viscum:a progress review.
China Journal of Chinese Materia Medica 2021;46(14):3551-3559
Viscum plants,the evergreen perennial parasitic shrubs or subshrubs,are mainly distributed in tropical and subtropical regions. There are about 70 Viscum species around the world,including 11 species and one variety in China. Mistletoe lectins are typeⅡ ribosome-inactivating proteins( RIPs) extracted from Viscum plants with anticancer and immunoregulatory activities. Many studies have focused on the mistletoe lectins isolated from V. album in Europe and V. album var. coloratum distributed in South Korea,respectively,and several preparations,such as Iscucin Ⓡ,were developed and clinically applied for cancer treatment. Although Viscum plants are widely distributed in China,only a few studies of mistletoe lectins have been reported. The recent progress of mistletoe lectins was reviewed from extraction,purification,quantitative/qualitative detection,molecular structure,pharmacological activities,toxicities,and clinical application,aiming at providing a reference for in-depth research and utilization of mistletoe lectins produced in China.
Humans
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Lectins
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Plant Extracts
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Plant Lectins
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Plant Proteins/genetics*
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Toxins, Biological
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Viscum
8.Change of Surface Carbohyd rate during Trans differentiation of Retinal Pigment Epithelial Cell.
Hee Seong YOON ; Sung Chur MOON ; Woo Jin JEUNG ; Hae Il PARK ; Young Hyun YOO
Journal of the Korean Ophthalmological Society 2000;41(4):838-846
This study was conducted to study the changes of cell surface carbohydrates during transdifferentiation of retinal pigment epithelial(RPE)cells. RPE cells were cultured from adult pig eyes. Surface carbohydrates of RPE cells from 1st, 3rd, 5th, 7th and 9th passages were assayed by lectin histochemistry and enzyme immunoassay. Changes in binding affinities to the lectins employed were demonsrated during trasdifferentiation of RPE cell. Whereas binding affinities of ConA, ECL, PNA, WGA, and UEA-I decreased graudally as the number of culture passage increased, binding properties to LCA, STL and DBA fluctuated depending on the number of passages. The results demonstrate changes of surface carbohydrates of RPE cell during trasdifferentiation. We suggest that changes of surface carbohydrates of RPE cell during trasdifferentiation may be close relations with the functional changes during transdifferentiation.
Adult
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Carbohydrates
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Epithelial Cells*
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Humans
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Immunoenzyme Techniques
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Lectins
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Retinaldehyde*
10.Characterization of the Multinucleated Giant Cell Glycoconjugates in the Tubercle of Human Pulmonary Tuberculosis.
Han Seok PARK ; Young Joon JIN ; Seo Young KO ; Young Hyun YOO ; Sik YOON
Korean Journal of Physical Anthropology 1997;10(2):169-179
Multinucleated giant cells (MGCs) are a prominent characteristic of granulomatous inflammation including tuberculosis. The present study was performed to investigate the characteristics and distribution pattern of intracellular and cell surface glycoconjugates of the MGCs in human pulmonary tubercles using lectin histochemistry. The cytoplasmic staining patterns could be divided into three groups. First, VVL, LCA and SBA showed intense reactivity in the great majority of the MGCs. Second, BS -I, DBA, WGA, PNA, ECL, PHA -L and PHA -E also showed positive staining in the cytoplasm of many MGCs, but the reaction patterns were not uniform. Third, the other group (BS -I - B4 and UEA -I) exhibited very weak or no staining in the cytoplasm. With regard to the membranous staining, the lectin binding patterns could be divided into two groups. First, WGA, ECL, PHA -L & PHA -E showed intense membranous staining. Second, the other lectins (BS -I, BS -I -B4, DBA, VVL, LCA, PNA, SBA and UEA -I) did not show any membranous staining. There was no significant difference in lectin binding patterns between the two types of MGCs. Our results demonstrated the characterization of glycoconjugates expressed in the MGCs in human pulmonary tubercles.
Cytoplasm
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Giant Cells*
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Glycoconjugates*
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Humans*
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Inflammation
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Lectins
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Tuberculosis
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Tuberculosis, Pulmonary*