An f-Type Thioredoxin from Arabidopsis thaliana Leaves

• 영문명: An f-Type Thioredoxin from Arabidopsis thaliana Leaves
• 발행기관: 강원대학교 기초과학연구소
• 저자명: Kim Tae-Soo Joon Chul Kim Chang Duck Jin Tae Jin Han Chang-Jin Lim
• 간행물 정보: 『기초과학연구』제10집, 143~148쪽, 전체 6쪽
• 주제분류: 자연과학 > 자연과학일반
• 파일형태: PDF
• 발행일자: 1999.12.01

영문 초록

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 chro-matography. The purified thioredoxin was determined to be a single band on SDS-PAGE, and its molecular 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+-nakate degtdrogenase. 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 μM on Escherichia coli 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 isolated from A. thaliana. Keywords: Arabidopsis thaliana, purification, thioredoxin

목차

Introduction

MATERIALS AND METHODS

RESULTS AND DISCUSSION

LITERATURE CITED