• Archives of Pharmacal Research
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• v.9 no.4
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• pp.201-203
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• 1986

Forty species of marine shells were collected from Korean coasts and studied extensively for their lectin activities by using erythrocytes of human blooc A, AB, B. O group and rabbit blood. In total, 7 species contained lectines :Neptunea intersculpta, Omphalius nigerrimus and Scapharca subcrenata, blood group nonspecific; Saxidomus purpuratus, human blood A and AB group specific; Lepidozona coreana, Tegilarca granosa and Neptunea polycosta, rabbit blood specific.

• YAKHAK HOEJI
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• v.40 no.4
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• pp.387-393
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• 1996

The erythrocytes agglutination test was applied to the common korean plants for lectin activity screening by using human blood. During the four years, 108 species from 46 families of floras were collected, identified and subjected to the test after being divided into several different parts. Only 13 species demonstrated strong lectin activities. Meanwhile 66 species did not shown any agglutination. All others were observed as having low activity or as having hemolytic constituents.

• YAKHAK HOEJI
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• v.31 no.4
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• pp.213-218
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• 1987

Twenty species of higher fungi growing in the wild were collected and studied extensively for their lectin activities by using erythrocytes of human, rabbit and mouse blood. In total, 14 species demonstrated hemagglutination with some kinds of erythrocytes. Of twenty species, eight (Boletus edulis, B. splendidus, Clavaria zollingeri, Lactaritis subzonarius, L. volemus, Russula cutefracta, Pholiota squarrosa, and P. aspera) were shown lymphoagglutination with murine splenic lymphocytes. Protein contents were estimated from the crude lectin fraction. Above mentioned eight species contained relatively high amounts of proteins than other mushrooms. Since these species had coincidently, hiig emagglutinating activity as well, we could define them as lectin-containeing mushrooms. Some species also contained mitogenic lectins toward murine splenic lymphocytes.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2000.05a
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• pp.530-530
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• 2000

The host defense system or immune system of all modern animals has their roots in very ancient organisms. After analyzing literature data concerning properties of invertebrates and vertebrates lectins we suggest that mechanism of mannans recognition may exist in marine invertebrates, as a universal mechanism for homeostasis maintenance and host defense, and mannan-binding lectins family of vertebrates has ancient precursor, as was shown for another S-type lectins family. We carried out the screening of mannan-binding type lectin among different species of echinoderms inhabiting in Piter the Grate Bay, the sea of Japan. As a result, the C-type lectins (SJL-32) specific for high mannose glycans was isolated from the coelomic plasma of the sea cucumbers Stichopus japonicus by ion-exchange chromatography on a DEAE-Toyopearl 650M, affinity chromatography on a mannan-Sepharose 6B and gel filtration on a Sephacryl S-200. SJL-32 is homodimer with molecular mass about 32 kDa on SDS-PAGE under non-reducing conditions. Protein part of the lectin has high conteins Asn, Glu, Ser. Hemagglutination of trypsin-treated O blood group human erythrocytes by SJL-32 was competitively inhibited by high-branched -D-mannan composed of -1,2 and -1,6 linked D-mannopyranose residues. In contrast, a variety of mono-, oligo-, and polysaccharides composed of residues of galactose and fucose showed absence or little inhibitory activities. The lectin activity strong depends on Ca2+ concentration, temperature and pH. Monospecific polyclonal antibodies were obtained to the lectin. As was shown by ELISA assay, antibodies to SJL-32 cross-reacted with human serum mannan-binding lectin. This data allows making conclusion about common antigenic determinants and structural homology of both lectins. In our opinion, SJL-32 belongs to evolutionary high conservative mannan-binding lectins (MBLs) family and takes part in the host defense against pathogenic microorganisms.

• YAKHAK HOEJI
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• v.31 no.2
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• pp.52-59
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• 1987

The result of the screening of lectins on 28 species of marine shell fishes(mollusks) showed that 10 species (Tapes philippinarum, Cyclosunetta menstrualis, Neptunea arthritica cumingii, Omphalius pfeifferi carpenteri, Chlorostoma argyrostoma turbinatum, Chiorostoma argyrostoma lischkei, Semisulcosira corea, Neptunea polycosta, Babylonica japonica, Noverita didyma) were present hemagglutinating properties to human A, B, and O group, and animal blood erythrocytes. A new lectin from Tapes philippinarum. was isolated and partially characterized. The lectin was purified by (NH$_4$)$_2$SO$_4$ precipitation and ion exchange chromatography on DE 53 column. Six fractions were obtained from DE 53 column by salt gradient elution but only 0.3M, and 0.4M NaCl fraction had strong lectin activity. On its 0.3M NaCl fraction, purity was identified by polyacrylamide gel electrophoresis. This lectin was inhibited by N-acetyl-D-galactosamine. It seems that two kinds of lectin react as antigen by immunochemical studies.