PURIFICATION OF FORM L(2)-RUBISCO FROM A MARINE OBLIGATELY AUTOTROPHIC HYDROGEN-OXIDIZING BACTERIUM, HYDROGENOVIBRIO-MARINUS STRAIN MH-110

被引：20

作者：

CHUNG, SY ^{[1
]}

YAGUCHI, T ^{[1
]}

NISHIHARA, H ^{[1
]}

IGARASHI, Y ^{[1
]}

KODAMA, T ^{[1
]}

机构：

[1] UNIV TOKYO, DEPT AGR CHEM, BUNKYO KU, TOKYO 113, JAPAN

来源：

FEMS MICROBIOLOGY LETTERS | 1993年 / 109卷 / 01期

关键词：

RIBULOSE BIS-PHOSPHATE CARBOXYLASE; L(2)-RUBISCO; HYDROGENOVIBRIO-MARINUS;

D O I：

10.1111/j.1574-6968.1993.tb06142.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO) was purified from an obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus MH-110. The protein has a M(r) value of approximately 110000, and is composed of two identical subunits of 55 000. To our knowledge, the existence of L2-form RubisCO in a chemolithoautotrophic bacterium is first reported in this paper. The N-terminal amino acid sequence determination of the purified enzyme showed high homology with those of the L2-form RubisCO of Rhodospirillum rubrum and the L(x)-form RubisCO from Rhodobacter sphaeroides.

引用

页码：49 / 54

页数：6