The structure of spinach ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) has been investigated by tilted-view electron microscopy of negatively stained monolayer crystals and image processing. The structure determined consists of a cylinder of octagonal cross-section with a large centr
β¦ LIBER β¦
Modulation of the tight binding of carboxyarabinitol 1,5-bisphosphate to the large subunit of ribulose 1,5-bisphosphate carboxylase/oxygenase
β Scribed by Alan V. Smrcka; Hans J. Bohnert; Richard G. Jensen
- Book ID
- 115708664
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 701 KB
- Volume
- 286
- Category
- Article
- ISSN
- 0003-9861
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Subunit arrangement of spinach ribulose
β
J. A. Barcena; P. J. Shaw
π
Article
π
1985
π
Springer-Verlag
π
English
β 879 KB
Molecular evolution of the large subunit
β
J.M. Shively; W. Devore; L. Stratford; L. Porter; L. Medlin; S.E. Stevens Jr.
π
Article
π
1986
π
John Wiley and Sons
π
English
β 665 KB
Formation of the tight-binding inhibitor
β
Genhai Zhu; Hans J. Bohnert; Richard G. Jensen; GΓΌnter F. Wildner
π
Article
π
1998
π
Springer
π
English
β 345 KB
Role of the small subunit in ribulose-1,
β
Robert J Spreitzer
π
Article
π
2003
π
Elsevier Science
π
English
β 518 KB
The CO2/O2specificity of ribulose 1,5-bi
β
Douglas B. Jordan; William L. Ogren
π
Article
π
1984
π
Springer-Verlag
π
English
β 623 KB
The substrate specificity factor, VcKo/ V o Kc, of spinach (Spinacia oleracea L.) ribulose 1,5-bisphosphate carboxylase/oxygenase was determined at ribulosebisphosphate concentrations between 0.63 and 200 gM, at pH values between 7.4 and 8.9, and at temperatures in the range of 5 ~ C to 40 ~ C. The
Affinity Purification of Ribulose-1,5-bi
β
P. Wang; M. Royer; R.L. Houtz
π
Article
π
1995
π
Elsevier Science
π
English
β 819 KB