BMB Reports
- Volume 28 Issue 1
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- Pages.62-67
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- 1995
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- 1976-670X(eISSN)
Purification and Characterization of Thioredoxin f from Pea Leaves
- Kang, Han-Chul (Department and Institute of Genetic Engineering, Kyunghee University) ;
- Hahn, Tae-Ryong (Department and Institute of Genetic Engineering, Kyunghee University)
- Published : 1995.01.31
Abstract
Thioredoxin f from pea leaves was purified to homogeneity and characterized. The purification steps involved ammonium sulfate fractionation, heat treatment, Sephadex G-75 and G-50 gel filtration, and hydroxyapatite and DEAE ion exchange chromatography. The monomeric molecular weight of purified pea thioredoxin f determined by SDS polyacrylamide gel electrophoresis was 12,000. The purified protein was active in the presence of reducing agents, such as dithiothreitol, at an alkaline pH (7.8~8.5). It was stable against heat such that more than 40% of its maximum activity remained after treatment at