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      • Purification, Characterization, and Synthesis of Vitellin from the Cabbage Butterfly, Pieris rapae L.

        고영규,김학렬,Ko, Yung-Gyu,Kim, Hak-Ryul 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4

        배추흰나비(Pieris rapae)의 vetellogenin과 vitellin을 전기영동을 이용하여 확인하였고 gel slice로 vitellin을 정제하여 vitellin의 물리화학적 성질들을 조사하였다. Vitellin은 등전점이 6.10이고 탄수화물, 지질, 인 등이 결합되어 있는 복합단백질로 나타났다. Vitellin은 nondenatured-PAGE로 결정된 분자량은 $380,000{\pm}10,000$ dalton이고 각각 150,000과 40,000 dalton의 분자량을 가지는 두 종류의 크고 작은 소단위로 구성된 구조를 지니는 것으로 나타났다. Double diffusion test와 Tandem-crossed immunoelectrophoresis에서 vitellogenin과 vitellin은 면역학적 동질성을 나타냈다. Rocket immunoelectrophoresis로 vitellogenesis 기간중 혈림프의 vitellogenin과 난소의 vitellin을 정량분석한 결과 vitellogenin과 vetellin은 용화 6일째 처음 나타난 이후 계속적으로 증가하였다. Juvenile hormone I은 용화 4일째의 암컷 지방체에서 vitellogenin을 합성시키도록 유도하였다. Vitellin from the cabbage butterfly, Pieris rapae L., was purified and characterized by electrophoresis. Vitellin from P. rapae is a phosphorylated glycolipoprotein of molecular weight of $380,000{\pm}10,000$ as determined by the nondenaturing polyacrylamide gel electrophoresis. Two subunits with $M_r$ of 150,000 and 40,000 were obtained from vitellin. The native molecule is thought to be a tetramer composed of two molecules of each of these subunits. The isoelectric point, as determined by isoelectric focusing on polyacrylamide gels, is 6.10. Vitellin and vitellogenin were indistinguishable by immunological methods such as double diffusion and tandem-crossed immunoelectrophoresis. Vitellogenin from the hemolymph and vitellin from the ovary were quantified by rocket immunoelectrophoresis. Vitellogenin and vitellin were first detected in 6-day-old pupae and their levels increased continuously during ovarian development. Vitellogein synthesis by the fat body in 4-day-old female pupae could be induced by juvenile hormone I.

      • SCIESCOPUSKCI등재

        배추흰나비 ( Pieris , rapae L . ) 의 vitellin 의 정제 , 물리화학적 성질 , 합성에 관한 연구

        고영규,김학렬 ( Yung Gyu Ko,Hak Ryul Kim ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4

        Vitellin from the cabbage butterfly, Pieris rapae L., was purified and characterized by electrophoresis. Vitellin from P. rapae is a phosphorylated glycolipoprotein of molecular weight of 380,000 ± 10,000 as determined by the nondenaturing polyacrylamide gel electrophoresis. Two subunits with MT of 150,000 and 40,000 were obtained from vitellin. The native molecule is thought to be a tetramer composed of two molecules of each of these subunits. The isoelectric point, as determined by isoelectric focusing on polyacrylamide gels, is 6.10. Vitellin and vitellogenin were indistinguishable by immunological methods such as double diffusion and tandem-crossed immunoelectrophoresis. Vitellogenin from the hemolymph and vitellin from the ovary were quantified by rocket immunoelectrophoresis. Vitellogenin and vitellin were first detected in 6-day-old pupae and their levels increased continuously during ovarian development. Vitellogein synthesis by the fat body in 4-day-old female pupae could be induced by juvenile hormone I.

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