• Title/Summary/Keyword: hemolymph

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Identification and Isolation of Juvenile Hormone Binding Protein from Hemolyrnph of Lymantria dispar L. (매미나방(Lymantria dispar)에서 Juvenile Hormone Binding Protein(JHBP)의 확인 및 정체)

  • 이인희;김학열
    • The Korean Journal of Zoology
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    • v.34 no.2
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    • pp.196-202
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    • 1991

  • Juvenile honnone binding protein (JHBP) was identified in the last instar larval hemolymph of Lymantria dispar using dextran coated charcoal (DCC) binding assay and gel filtration. The p1 value of JHBP was estimated to be 5.3. JHBP was partially pudfied by polyethylene glycol(PEG) precipitation, DEAE-cellulose ion-exchange chromatography and gel filtration, and was confirmed by DCC binding assay.

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Lymphocytes Mitogenic and Immunochemical Characteristics of the Immunomodulating Lectins, MLA, from Marine Natural Products (해양 천연물에서 분리한 면역기능 조정제 렉틴 MLA의 림프구 자극분열효과 및 면역화학적 특성)

  • 전경희;김장환;정시련
    • YAKHAK HOEJI
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    • v.39 no.3
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    • pp.252-259
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    • 1995

  • Isolation, purification and characterization of biophysicochemical properties of the three new lectins, MLA-I, MLA-II, MLA-III from the hemolymph of Meretrix lusoria have been reported previously. A series of immunochemical studies were investigated in this work. The three lectins were revealed as having partial identity each other by immunodiffusim and immunoelectrophoresis. These results suggest that MLA lectins are isolectins having similar biophysicochemical properties. Particularly, MLA-I proved to be a potent mitogen for murine splenic as well as human peripheral lymphocytes, and the optimum mitogenic dose were 62.5 and 1.95 $\mu\textrm{g}$/ml, respectively.

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Immunostimulating Lectins from Marine Natural Products: Characteristics of the MLA-I, MLA-II and MLA-III (해양 천연물로부터 면역기능 조정제 렉틴 개발 : MLA-I, MLA-II, MLA-III의 특성)

  • 정시련;김장환;전경희
    • YAKHAK HOEJI
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    • v.39 no.3
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    • pp.243-251
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    • 1995

  • Three new lectins, MLA-I, MLA-II and MLA-III, have been isolatedand purified from the hemolymph of Meretrix lusoria and reported previously. Biophysicochemical characteristics were investigated with these three MLA lectins. The MLA lectins agglutinated human erythrocytes non specifically and proved as D-galactose group carbohydrate specific. Molecular weight of ML.A-I. II and III were estimated to be 330, 500 and 310KD, respectively, by gel filtration on Sepharose CL-6B column. On SDS-polyacrylamide gel electrophoresis, ML.A-I was dissociated into a single subunit of 42KD, MLA-II was into the twelve subunits of 46, 32, 30, 28, 25, 23. 22, 20. 19, 16, 15, and 14KD, and MLA-III was into the two subunits of 72 and 44KD. The pl of MLA-I, II, III were 4.0. 4.9 and 5.0. Amino acid analysis revealed a high contents of acidic and hydroxy amino acids, and a paucity of sulfur containing amino acids. Proline was not contained in MLA-II.

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