SUBCELLULAR-LOCALIZATION AND PROPERTIES OF L-GALACTONO-GAMMA-LACTONE DEHYDROGENASE IN SPINACH LEAVES

被引：35

作者：

MUTSUDA, M ^{[1
]}

ISHIKAWA, T ^{[1
]}

TAKEDA, T ^{[1
]}

SHIGEOKA, S ^{[1
]}

机构：

[1] KINKI UNIV, DEPT FOOD & NUTR, NARA 631, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1995年 / 59卷 / 10期

关键词：

D O I：

10.1271/bbb.59.1983

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

L-Galactono-gamma-lactone dehydrogenase, which catalyzes the final step of the biosynthesis of L-ascorbate, is bound to spinach mitochondrial membrane, as confirmed by linear sucrose density gradient centrifugation. The solubilized enzyme was very labile, but stabilized in the presence of L-galactono-gamma-lactone under anaerobic conditions. The enzyme reduced cytochrome c and phenazine methosulfate in the presence of L-galactono-gamma-lactone, but not when L-gulono-gamma-lactone was used as an electron donor. The K(m)s of the enzyme for L-galactono-gamma-lactone and cytochrome c were 192 mu M and 180 mu M, respectively.

引用

页码：1983 / 1984

页数：2

共 20 条

[1]

LIGHT-DEPENDENT REDUCTION OF DEHYDROASCORBATE AND UPTAKE OF EXOGENOUS ASCORBATE BY SPINACH-CHLOROPLASTS [J].