期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：2002
卷号：48
期号：3
页码：242-246
DOI：10.3177/jnsv.48.242
出版社：Center for Academic Publications Japan
摘要：Summary High activity (about 50 mU⋅mg protein-1) of methylmalonyl-CoA mutase (82-95% apo-enzyme) was constantly found during the cell growth of a methanol-utilizing bacterium, Methylobacterium extorquens NR-1. The apo-enzyme was purified to homogeneity and characterized. The purified enzyme was colorless. An apparent Mr of M. extorquens NR-1 enzyme was calculated to be 150, 000±5, 000 by Superdex 200 HR gel filtration. SDS-polyacrylamide gel electrophoresis of the purified enzyme gave two protein bands with an apparent Mr of 85, 000±2, 000 and 70, 000±2, 000, indicating that the M. extorquens NR-1 enzyme is composed of two nonidentical subunits. NH2-terminal amino acid sequences of the small and large subunits of M. extorquens NR-1 enzyme showed no significant homology to those of the enzyme from other species. Some enzymological properties of the M, extorquens NR-1 enzyme were studied.
