Purification and characterization of phosphoribulokinase from the cyanobacterium Synechococcus PCC7942.
作者信息
Wadano A, Kamata Y, Iwaki T, Nishikawa K, Hirahashi T
机构信息
Department of Applied Biochemistry, University of Osaka Prefecture, Japan.
出版信息
Plant Cell Physiol. 1995 Oct;36(7):1381-5.
PMID:8564307
Abstract
Phosphoribulokinase (PRK) was purified to electrophoretic homogeneity from Synechococcus PCC7942 with high specific activity. Molecular masses of the native enzyme and its subunit were 178 and 42 kDa, respectively. Cys-17 and Cys-38 were conserved in the cyanobacterial PRK, but 18 amino acid residues between them were missing among the 40 residues found in higher plant PRKs.
摘要
Zotero 插件