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한국식물학회 / v.41, no.4, 1998년, pp.312-317 
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( An f-Type Thioredoxin from Arabidopsis thaliana Leaves ) |
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| 초 록 |
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| Thioredoxin, a small redox protein with an active site disulfide/dithiol, is ubiquitous in bacteria, plants, and animals and functions as a reducing agent and modulator of enzyme activity. A thioredoxin has been purified to electrophoretic homogeneity from the leaves of Arabidopsis thaliana using procedures such as DE-52 ion exchange chromatography, Sephadex G-50 gel filtration, Q-Sepharose ion exchange chromatography, and DEAE-Sephadex A-25 chromatography. The purified thioredoxin was determined to be a single band on SDS-PAGE, and its moleculr weight was estimated to be 21 KDa, which was much larger than those of most other known thioredoxins. It was proved to be an f-type thioredoxin, since it could activate fructose-1, 6-bisphosphatase, but it could not activate NADP+-malate dehydrogenase. As a protein disulfide reductase, it could reduce the disulfide bonds contained in insulin. As a substrate, it showed a Km value of 20.2 ulcornerM on Escherichia coil thioredoxin reductase, and it had an optimal pH of 8.0. The molecular weight of the purified f-type thioredoxin is not consistent with those of the five divergent h-type thioredoxins already identified by cDNA cloning. The purified f-type thioredoxin is the first example isolate from A. thaliana. |
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| 키워드 |
| Arabidopsis thaliana;purification;thioredoxin; |
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Journal of Plant Biology / v.41, no.4, 1998년, pp.312-317
한국식물학회
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199811920119329)
언어 : 영어 |
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| 논문 제공 : KISTI 한국과학기술정보연구원 |
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