• 제목/요약/키워드: Hemolymph

검색결과 244건 처리시간 0.046초

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

  • 이인희;김학열
    • 한국동물학회지
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    • 제34권2호
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    • pp.196-202
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    • 1991

  • 매미나방 종령유층 혈림프내에 존재하는 JHBP을 Dextran Coated Charcoal (DCC)binding assay와 gel filtration에 의해서 확인하였고, JHBP의 pI값은 5.3으로 밝혀졌다. JHBP의 정저는 혈림프단백질을 먼저 PEG로 침전시킨 후 ion exchange chromatography와 gel filtration 방법을 통하여 행하였다. 정체된 fraction의 JH에 대한 binding activity는 [3H] JH-III의 radioactivity 측정과 DCC binding assay를 통해 확인하였고, 정체된 단백질의 순수도는 각 정체단계에 따라 전지영동을 하여 확인하였다.

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

  • 전경희;김장환;정시련
    • 약학회지
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    • 제39권3호
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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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해양 천연물로부터 면역기능 조정제 렉틴 개발 : MLA-I, MLA-II, MLA-III의 특성 (Immunostimulating Lectins from Marine Natural Products: Characteristics of the MLA-I, MLA-II and MLA-III)

  • 정시련;김장환;전경희
    • 약학회지
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    • 제39권3호
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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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