Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Uemura, K.
Right arrow Articles by Yokota, A.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Uemura, K.
Right arrow Articles by Yokota, A.
Agricola
Right arrow Articles by Uemura, K.
Right arrow Articles by Yokota, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1996, Vol. 37, No. 3 325-331
© 1996

A Rapid and Sensitive Method for Determination of Relative Specificity of RuBisCO from Various Species by Anion-Exchange Chromatography

Koichi Uemura1,4, Yoshihiro Suzuki1, Toshiharu Shikanai1,5, Akira Wadano2, Richard G. Jensen3, Wendy Chmara3 and Akiho Yokota1,6

1Plant Molecular Physiology Laboratory, Research Institute of Innovative Technology for the Earth (RITE) Kizu, Kyoto, 619-02 Japan
2Department of Agricultural Chemistry, University of Osaka Prefecture Sakai, Osaka, 591 Japan
3Department of Biochemistry and Plant Science, University of Arizona Tucson, Arizona 85721, U.S.A.

6To whom correspondence should be addressed.

A rapid and sensitive method to determine the relative specificity ({tau}) of ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) using anion-exchange chromatography is described. We employed the open gas system for the reaction of RuBisCO to get the most reliable CO2 and O2 concentrations in the reaction mixture. 3-Phosphoglycerate and 2-phosphoglycolate which were formed in the RuBisCO reaction were completely separated and directly measured with anion-exchange chromatography without using radioisotopes. The determination of the {tau} value was accomplished in 3 h. The {tau} values of RuBisCO enzymes from higher land plants were between 90 and 96, and those from bacteria including cyanobacterium were close to 45. These values were in agreement with previously reported values. The enzyme of the red macroalga Porphyra yezoensis exhibited a {tau} value of over 140, as expected from the reported value of the enzyme from the red microalga Porphyridium cruenteum. RuBisCO from the green macroalga Ulva pertusa had a {tau} value close to 70 and similar to that of the enzyme from the green microalga Chlamydomonas reinhardtii.

4On leave from Research and Development Center, Unitika Ltd., 23 Kozakura, Uji, Kyoto, 611 Japan.

5Present address: Nara Institute of Science and Technology, 8916-5 Takayama-Cho, Ikoma, Nara, 630-01 Japan

(Received December 26, 1995; Accepted February 7, 1996)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J Exp BotHome page
H. Griffiths, W. E. Robe, J. Girnus, and K. Maxwell
Leaf succulence determines the interplay between carboxylase systems and light use during Crassulacean acid metabolism in Kalanchoe species
J. Exp. Bot., May 1, 2008; 59(7): 1851 - 1861.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
S. Yoshida, H. Atomi, and T. Imanaka
Engineering of a Type III Rubisco from a Hyperthermophilic Archaeon in Order To Enhance Catalytic Performance in Mesophilic Host Cells
Appl. Envir. Microbiol., October 1, 2007; 73(19): 6254 - 6261.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
M. A. J. Parry, P. J. Andralojc, R. A. C. Mitchell, P. J. Madgwick, and A. J. Keys
Manipulation of Rubisco: the amount, activity, function and regulation
J. Exp. Bot., May 1, 2003; 54(386): 1321 - 1333.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Sugawara, H. Yamamoto, N. Shibata, T. Inoue, S. Okada, C. Miyake, A. Yokota, and Y. Kai
Crystal Structure of Carboxylase Reaction-oriented Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase from a Thermophilic Red Alga, Galdieria partita
J. Biol. Chem., May 28, 1999; 274(22): 15655 - 15661.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Ezaki, N. Maeda, T. Kishimoto, H. Atomi, and T. Imanaka
Presence of a Structurally Novel Type Ribulose-bisphosphate Carboxylase/Oxygenase in the Hyperthermophilic Archaeon, Pyrococcus kodakaraensis KOD1
J. Biol. Chem., February 19, 1999; 274(8): 5078 - 5082.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.