• Title/Summary/Keyword: Marine animal lectins

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Studies on Lectins from Marine Animal Chlorostoma argyrostoma turbinatum (해양동물 구멍밤고둥의 렉틴 성분 연구)

  • Chung, See-Ryun;Choi, Il-Shik;Jeune, Kyung-Hee
    • Korean Journal of Pharmacognosy
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    • v.25 no.2
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    • pp.121-131
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    • 1994
  • Two kinds of new lectins, CATL-I and CATL-II, were partially purified from the intestine of Chlorostoma argyrostoma turbunatum by physical saline extraction, salt fractionation, ion exchange chromatography and gel filtration. CATL-I and CATL-II were purified 39.4 and 15.8 fold with a yield of 8.8 and 7.4%, respectively. On polyacrylamide gel electrophoresis, CATL-I demonstrated one major and one minor bands. This lectin agglutinated human and other animal erythrocytes nonspecifically and also agglutinated murine splenic lymphocytes. Carbohydrate specificity of the lectins was determined by inhibition of the agglutinability by methyl-${\alpha}-_D$-galactopyranoside and $_L-rhamnose$ at a final concentration of 6 mM. The lectins contained relatively high amounts of acidic amino acids, but the contents of sulfur containing amino acids were very low or was not estimated. Immunochemical studies were carried out to identify some properties of marine animal lectins.

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Lymphocytes Mitogenic and Immunochemical Properties of the Lectins from Marine Animal Lunella coronata coreensis (해양동물 눈알고둥 렉틴의 림프구 분열효과 및 면역화학적 특성)

  • 소명숙;전경희;정시련
    • YAKHAK HOEJI
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    • v.37 no.3
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    • pp.254-261
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    • 1993
  • Developing new substance for immunosuppressor or immunomodulator from natural products is extremely important in the present biomedicine. In this paper, we focused our efforts on the mitogenicity and immunochemical properties of the two lectins (LCC-I, LCC-II) obtained from marine animal Lunella coronata coreensis. Immunochemical techniques were employed to elucidate the structural and/or functional similarities between the LCC lectins. Molecular weight of the LCC lectins, LCC-I and LCC-II were estimated to be around 60 KD and 66-70 KD, respectively. LCC lectins were mitogens for murine splenic lymphocytes, and the optimum mitogenic doses were 31.25 $\mu\textrm{g}$/ml and 3.91 $\mu\textrm{g}$/ml, respectively. LCC-II lectin was a good mitogen toward human peripheral lymphocytes at a concentration about 31.25 $\mu\textrm{g}$/ml.

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Studies on Lectins from Marine Shells (III) : Screening of Lectin-like Agglutinins from Marine Shells

  • Chung, See-Ryun;Kim, Jang-Hwan;Suh, Young-Ah;Jeunechung, Kyung-Hee
    • 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.

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Studies on Lectins From Marine Shells (V) - Isolation and Purification of Letin from Tapes philippinarum. (해양 패류 렉틴성분 연구 (V) - 반지락조개의 렉틴성분 분리정제에 관한 연구)

  • 정시련;김장환;전경희
    • 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.

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