Characterization of Thioltransferase from Kale

• 영문명: Characterization of Thioltransferase from Kale
• 발행기관: 강원대학교 기초과학연구소
• 저자명: Jae-Hoon Sa Mi-Young Yang Byung-Lim Song Chang-Jin Lem
• 간행물 정보: 『기초과학연구』제8집, 16~27쪽, 전체 12쪽
• 주제분류: 자연과학 > 자연과학일반
• 파일형태: PDF
• 발행일자: 1997.12.01

영문 초록

Thioltransferase, also known as glutaredoxin, is an enzyme that catalyzes the reduction of a variety of disulfides, including protein disulfides, in the presence of reduced glutathione. Thioltransferase was purified from kale through ammonium sulfate fractionation, DE-52 ion-exchange chromatography, Sephadex G-75 gel filtration, and Q-Sepharose ion-exchange chromatography. Its molecular size was estimated to be about 13,000 daltons on SDS- PAGE. The purified enzyme has an optimum pH of about 8.0 with 2-hydroxyethyl disulfide as a substrate. The enzyme also utilizes L-sulfocysteine, L-cystine, bovine serum albumin, and insulin as substrates in the presence of GSH. The enzyme has Km values of 0.24-0.67 mM against these substrates. The enzyme was partly inactivated after heating at 80℃ or higher temperature. The enzyme was greatly activated by various thiol compounds such as reduced glutathione, dithiothreitol, L-cysteine and β-mercaptoethanol. This is a second example of plant thioltransferase, which was purified and characteried

목차

Abstract

Introduction

Materials and Methods

Results and Discussion

Acknowledgement

References