INSITU ASSAY OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE IN THIOBACILLUS-NEAPOLITANUS

被引：15

作者：

CANNON, GC ^{[1
]}

ENGLISH, RS ^{[1
]}

SHIVELY, JM ^{[1
]}

机构：

[1] CLEMSON UNIV, DEPT BIOL SCI, CLEMSON, SC 29634 USA

来源：

JOURNAL OF BACTERIOLOGY | 1991年 / 173卷 / 04期

关键词：

D O I：

10.1128/jb.173.4.1565-1568.1991

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Cells permeabilized with chloroform yielded ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) activities nearly equal to those of cell extracts, thus indicating that both cytoplasmic and carboxysomal RuBisCO are functional in situ. The carboxysomal and cytoplasmic RuBisCO both form the CO2-Mg2+-enzyme ternary complex, as evidenced by stabilization with 2-C-carboxy-D-arabinitol-1,5-bisphosphate (CABP), a potent competitive inhibitor of RuBisCO. The data are consistent with the hypothesis that the carboxysome is functional in carbon dioxide fixation.

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页码：1565 / 1568

页数：4

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