Purification and properties of nitrite reductase from the blue-green alga Anabaena cylindrica

スポンサーリンク

概要

• 論文の詳細を見る

• Nitrite reductase was purified about 40-fold the blue-green alga Anabaena cylindrica by acetone precipitation and chromatography on DEAE-cellulose columns. The nitrite reductase had its pH optima at about 7.6 with Tris-HCI and at about 7.4 with phosphate when reduced methyl viologen was used as an electron donor. The K_m's for nitrite, methyl viologen and ferredoxin were 5×10^<-5>, 2×10^<-4> and 5×10^<-6>M, respectively. A stoichiometry of one molecule of ammonia formation per one molecule of nitrite disappearance was confirmed. Ferredoxin which had been reduced either chemically with dithionite or enzymatically with NADPH in the presence of diaphorase was active as an electron donor. Dithionite-reduced FAD and FMN were inactive. NADPH could not give electrons directly to nitrite reductase. Hydroxylamine reductase was segregated from nitrite reductase by DEAE-cellulose column chromatography. Purified nitrite reductase showed no activity for sulfite reduction. A molecular weight of 68,000 was estimated for nitrite reductase using a calibrated Sephadex G-200 column.

• 日本植物生理学会の論文

著者

• Hattori Akihiko

  The Ocean Research Institute University Of Tokyo

• UESUGI IZUMI

  Institute of Applied Microbiology, University of Tokyo

• Uesugi Izumi

  Institute Of Applied Microbiology University Of Tokyo:(present)department Of Botany Faculty Of Scien

関連論文

• Purification and properties of nitrite reductase from the blue-green alga Anabaena cylindrica

スポンサーリンク