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RISS 인기검색어
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- 저자 : 유기중 ( Chun Yung Lee (검색결과 3 건)
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녹두(Phaseolus aureus)와 팥(Phaseolus angularis)의 저장단백질의 분리와 그 특성에 관하여
이춘영,김수언,유기중,Lee, Chun-Yung,Kim, Soo-Un,Yoo, Ki-Jung 생화학분자생물학회 1978 한국생화학회지 Vol.11 No.3
녹두(P.aureus)와 팥(P.angularis)의 저장단백질을 Sephadex G-150으로 크로마토그라피하여 분리하고 그의 전기영동상 특성을 연구하였다. 분리된 단백질은 잠정적으로 Fl globulin 과 F2 globulin 으로 명명하였는데 각각 legumin과 vicilin으로 동정되었다. F2 globulin은 주 저장단백질로서 당단백질이었으며 disc-전기영동에서 확산된 하나의 분리대로 나타났다. 한편 SDS-전기영동과 PAW-전기영동에서는 작은 분리대 몇개가 주분리대와 함께 나타났다. SDS-전기영동에서 나타난 다섯 주분리대의 겉보기 분자량은 녹두에서 64,000, 53,000, 50,000, 27,000 그러고 23,400 이었으며 팥에서는 55,300, 53,000, 29,600, 26,600 그리고 25,000 이었다. A successful fractionation of the storage proteins in mung bean (P. aureus) and small red bean (P. angularis) seeds with chromatography on Sephadex G-150 was attained. Isolated proteins, tentatively designated as F2 globulin and F1 globulin, were classified as vicilin and presumably as legumin, respectively. Disc-PAGE of the major storage protein, F2 globulin, displayed a diffused band stained with periodic acid-Schiff's base reagent. However, SDS-PAGE demonstrated the faint bands besides five major bands. Apparent molecular weights of each subunit determined with SDS-PAGE were 64,000, 53,000, 50,000, 27,000 and 23,400 in F2 globulin of the mung bean and 55,300, 53,000 29,600, 26,600 and 25,000 in small red bean.
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녹두 ( Phaseolus aureus ) 와 팥 ( Phaseolus angularis ) 의 저장단백질의 분리와 그 특성에 관하여
이춘영,김수언,유기중 ( Chun Yung Lee,Soo Un Kim,Ki Jung Yoo ) 생화학분자생물학회 1978 BMB Reports Vol.11 No.3
A successful fractionation of the storage proteins in mung bean (P. aureus) and small red bean (P. angularis) seeds with chromatography on Sephadex G-150 was attained. Isolated proteins, tentatively designated as F2 globulin and F1 globulin, were classified as vicilin and presumably as legumin, respectively. Disc-PAGE of the major storage protein, F2 globulin, displayed a diffused band stained with periodic acid-Schiff`s base reagent. However, SDS-PAGE demonstrated the faint bands besides five major bands:.Apparent molecular weights of each subunit determined with SDS-PAGE were 64,000 53,000. 50,000. 27,000 and 23,400 in F2 globulin of the mung bean and 55,300. 53,000 29,600 26,600 and 25,000 in small red bean.
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이춘영,유기중 한국농화학회 1982 Applied Biological Chemistry (Appl Biol Chem) Vol.25 No.1
The total protein, peroxidase and isocitrate lyase of ungerminated seeds and germinated seedlings of Sesamum indicum L. were studied by disc polyacrylamide get electrophoresis. In the electrophoretic studies of ungerminated seed proteins, more than 13 bands were observed by amido black 10B staining. Among 13 protein hands, 4 bands showed peroxidase activity and 4 bands isocitrate lyase activity. During germination it was noted that there were some changes in protein levels within the bands. Proteins with low electrophoretic mobilities increased within 19 hours and decreased after 45 hours, while those with high mobilities remained fairly constant. Protein band sharpness decreased with germination.. During germination the number of peroxidase isozymes increased from 4 to 5 within 45 hours and to 6 in 97 hours. The enzyme activity of each band (except for one hand between 65 and 97 hours) increased with germination and was more apparent after 45 hours. The number of isozymes in isocitrate lyase did not appear to change during germination. The enzyme activity of each bard decreased with germination and disappeared after 45 hours.
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