(A) study on lipoxygenase from soybean = 대두의 lipoxygenase 에 관한 연구

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Soybean lipoxygenase (E.C.1.13.11.12) was purified by ammonium sulfate fractionation, affinity chromatography on linoleate-aminohexyl Sepharose 4B and DEAE-cellulose chromatography. Purification of lipoxygenase-2 through affinity chromatography at PH 6.8 resulted in 6-fold purification and yield of 91%. However, linoleate-aminoethyl Sepharose 4B did not retain a significant amount of lipoxygenase. Further purification was conducted through DEAE-cellulose chromatography with the factor of 4-fold, and the yield was 46 % with respect to lipoxygenase-2. Overall purification of lipoxygenase-2 was 32.4-fold, and yield was 28.5 %. The purfied lipoxygenase-2 was almost homogeneous, electrophoretically. The Km values of lipoxygenase-1 and -2 for linoleic acid were 0.15 mM and 0.39 mM, respectively. And the activation energies of the reactions catalyzed by lipoxygenase-1 and -2 were 16.2 kcal/mole and 39.6 kcal/mole, respectively. Molecular weight of lipoxygenase was determined from gel chromatography on Sephadex G-150 to be 102,000. When lipoxygenase-2 was subjected to be reacted with arachidonic acid, and subsequently reduced with sodium dithionite, a material from ether extracts of this reaction mixture seemed to have some of prostaglandin F_{2α}, which was identified through thin layer chromatography.
Advisors
Byun, Si-Myung변시명
Description
한국과학기술원 : 생물공학과,
Publisher
한국과학기술원
Issue Date
1980
Identifier
62632/325007 / 000781014
Language
eng
Description

학위논문 (석사) - 한국과학기술원 : 생물공학과, 1980.2, [ viii, 67 p. ]

Keywords

단백질 분리.

URI
http://hdl.handle.net/10203/27834
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=62632&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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