A rapid and sensitive method for determination of relative specificity of RuBisCO from various species by anion-exchange chromatography

Plant and Cell Physiology

Volumn 37, Issue 3, 1996, Pages 325-331

  Uemura, Koichi ^a,d   Suzuki, Yoshihiro ^a   Shikanai, Toshiharu ^a,e   Wadano, Akira ^b   Jensen, Richard G ^c   Chmara, Wendy ^c   Yokota, Akiho ^a  

^a RESEARCH INSTITUTE OF INNOVATIVE TECHNOLOGY FOR THE EARTH   (Japan)

^b Osaka Prefecture University   (Japan)

^c UNIVERSITY OF ARIZONA   (United States)

^d UNITIKA LTD   (Japan)

^e NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

Anion exchange chromatography; Assay; Porphyra yezoensis; Relative specificity; Ribulose 1,5 bisphosphate carboxylase oxygenase (EC 4.1.1.39); Specificity factor

Indexed keywords

EID: 0000542974     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.pcp.a028949     Document Type: Article

References (30)

1. Andrews, T.J. (1988) Catalysis by cyanobacterial ribulosebisphosphate carboxylase large subunits in the complete absence of small subunits. J. Biol. Chem. 263: 12213-12220.
2. Andrews, T.J. and Lorimer, G.H. (1987) Rubisco: structure, mechanisms, and prospects for improvement. In The Biochemistry of Plants. Volume 10. Edited by Hatch, M.D. and Boardman, N.K. pp. 131-218. Academic Press, New York.
3. Badger, M.R., Kaplan, A. and Berry, J.A. (1980) Internal inorganic carbon pool of Chlamydomonas reinhardtii: evidence for a carbon dioxide concentrating mechanism. Plant Physiol. 66: 407-413.
4. Badger, M.R. and Lorimer, G.H. (1981) Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylase. Biochemistry 20: 2219-2225.
5. 2 specificity of ribulose-1,5-bisphosphate carboxylase/oxygenase and the rate of respiration in the light-estimates from gas-exchange measurements on spinach. Planta 165: 397-406.
6. Christeller, J.T. and Tolbert, N.E. (1978) Phosphoglycolate phosphatase. J. Biol. Chem. 253: 1780-1785.
7. 4: Mechanisms, and Cellular and Environmental Regulation, of Photosynthesis, p. 33. Blackwell Scientific Publications, Oxford.
8. 3 species. Planta 149: 78-90.
9. Gorman, D.S. and Levine, R.P. (1965) Cytochrome f and plastcyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA 54: 1665-1669.
10. 2+ induced by chloroplast intermediates. Arch. Biochem. Biophys. 205: 587-594.
11. Hartman, F.C. (1992) Structure-function relationships of ribulosebisphosphate carboxylase/oxygenase as suggested by site-directed mutagenesis. In Plant Protein Engineering. Volume 1. Edited by Shewry, P.R. and Gutteridge, S. pp. 61-92. Cambridge University Press, London.
12. 2 specificity determination and idintification of side products. Anal. Biochem. 209: 367-374.
13. Jordan, D.B. and Ogren, W.L. (1981) Species variation in the specificity of ribulose bisphosphate carboxylase/oxygenase. Nature 291: 513-515.
14. 2 specificity of ribulosebisphosphate carboxylase-oxygenase. Aust. J. Plant Physiol. 21: 449-461.
15. Kent, S.S. and Tomany, M.J. (1984) Kinetic variance of ribulose-1,5-bisphosphate carboxylase/oxygenase isolated from diverse taxonomic sources. Plant Physiol. 75: 645-650.
16. 2 specificity factor. Photosynth. Res. 43: 57-66.
17. 2, and ribulose-1,5-diphosphate carboxylase. Plant Physiol. 54: 678-685.
18. Murashige, T. and Skoog, F. (1962) A revised medium for rapid growth and bioassay with tabacco tissue cultures. Physiol. Plant. 15: 473-479.
19. 2. J. Exp. Bot. 40: 317-320.
20. Read, B.A. and Tabita, F.R. (1994) High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eukaryotic marine algae and properties of recombinant cyanobacterial rubisco containing "algal" residue modifications. Arch. Biochem. Biophys. 312: 210-218.
21. Spreitzer, R.J. (1993) Genetic dissection of rubisco structure and function. Annu. Rev. Plant Physiol. Plant Mol. Biol. 44: 411-434.
22. Tolbert, N.E. (1980) Photorespiration. In The Biochemistry of Plants. Volume 2. Edited by Stumpf, P.K. and Conn, E.E. pp. 487-523. Academic Press, New York.
23. Viale, A.M., Kobayashi, H. and Akazawa, T. (1990) Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum. J. Biol. Chem. 265: 18386-18392.
24. 3 plants. Aust. J. Plant. Physiol. 18: 287-305.
25. von Caemmerer, S., and Evans, J.R., Hudson, G.S. and Andrews, T.J. (1994) The kinetics of ribulose-1,5-bisphosphate carboxylase/oxygenase in vivo inferred from measurements of photosynthesis in leaves of transgenic tobacco. Planta 195: 88-97.
26. Wilhelm, E., Battino, R. and Wilcock, R.J. (1977) Low-pressure solubility of gases in liquid water. Chem. Rev. 77: 219-262.
27. Yokota, A. (1991) Ribulose bisphosphate-induced, slow conformational changes of spinach ribulose bisphosphate carboxylase cause the two types of inflections in the course of its carboxylase reaction. J. Biochem. 110: 246-252.
28. 2 conditions in Chlorella pyrenoidosa. Plant Physiol. 80: 341-345.
29. Yokota, A. and Kitaoka, S. (1989) Linearity and functioning forms in the carboxylase reaction of spinach ribulose 1,5-bisphosphate carboxylase/ oxygenase. Plant Cell Physiol. 30: 183-191.
30. 14C]glycreate 3-phosphate. Plant Physiol. 98: 764-768.