Abstract
Extraction of maize (Zea mays) leaves by progressive grinding under suitably protective conditions yields total carbonic anhydrase activities (4800 units per milligram chlorophyll) comparable to the activity in spinach (Spinacia oleracea) leaves. The total ribulose diphosphate carboxylase activity was also equal to or greater than the best literature values for maize. Of the total leaf carbonic anhydrase, 72.5% on a chlorophyll basis was present in the mesophyll cells and 14.2% in the bundle-sheath cells. The distribution of the total leaf ribulose diphosphate carboxylase between the mesophyll and bundle-sheath cells was 42.0 and 48.7% respectively. There was three times as much total chlorophyll in extracts of the mesophyll cells compared with the bundle-sheath cells of maize. Similar results for the above distribution of the two enzymes were found using a differential grinding technique. The possible function of carbonic anhydrase in photosynthesis is discussed. The equal distribution of ribulose diphosphate carboxylase activity between the mesophyll and bundle-sheath cells casts doubt upon the hypothesis that a rigid biochemical compartmentation exists between these cell types in maize.
Full text
PDF




Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BRUINSMA J. A comment on the spectrophotometric determination of chlorophyll. Biochim Biophys Acta. 1961 Sep 30;52:576–578. doi: 10.1016/0006-3002(61)90418-8. [DOI] [PubMed] [Google Scholar]
- Chen T. M., Brown R. H., Black C. C. Photosynthetic CO(2) Fixation Products and Activities of Enzymes Related to Photosynthesis in Bermudagrass and Other Plants. Plant Physiol. 1971 Feb;47(2):199–203. doi: 10.1104/pp.47.2.199. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cooper T. G., Filmer D. The active species of "CO2" utilized by ribulose diphosphate carboxylase. J Biol Chem. 1969 Feb 10;244(3):1081–1083. [PubMed] [Google Scholar]
- Cooper T. G., Wood H. G. The carboxylation of phosphoenolpyruvate and pyruvate. II. The active species of "CO2" utilized by phosphoenlpyruvate carboxylase and pyruvate carboxylase. J Biol Chem. 1971 Sep 10;246(17):5488–5490. [PubMed] [Google Scholar]
- Graham D., Reed M. L. Carbonic anhydrase and the regulation of photosynthesis. Nat New Biol. 1971 May 19;231(20):81–83. doi: 10.1038/newbio231081a0. [DOI] [PubMed] [Google Scholar]
- Hatch M. D. The C 4 -pathway of photosynthesis. Evidence for an intermediate pool of carbon dioxide and the identity of the donor C 4 -dicarboxylic acid. Biochem J. 1971 Nov;125(2):425–432. doi: 10.1042/bj1250425. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Paulsen J. M., Lane M. D. Spinach ribulose diphosphate carboxylase. I. Purification and properties of the enzyme. Biochemistry. 1966 Jul;5(7):2350–2357. doi: 10.1021/bi00871a025. [DOI] [PubMed] [Google Scholar]
- Poincelot R. P. Intracellular distribution of carbonic anhydrase in spinach leaves. Biochim Biophys Acta. 1972 Feb 28;258(2):637–642. doi: 10.1016/0005-2744(72)90255-0. [DOI] [PubMed] [Google Scholar]
- Slack C. R., Hatch M. D., Goodchild D. J. Distribution of enzymes in mesophyll and parenchyma-sheath chloroplasts of maize leaves in relation to the C4-dicarboxylic acid pathway of photosynthesis. Biochem J. 1969 Sep;114(3):489–498. doi: 10.1042/bj1140489. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Woo K. C., Anderson J. M., Boardman N. K., Downton W. J., Osmond C. B., Thorne S. W. Deficient Photosystem II in Agranal Bundle Sheath Chloroplasts of C(4) Plants. Proc Natl Acad Sci U S A. 1970 Sep;67(1):18–25. doi: 10.1073/pnas.67.1.18. [DOI] [PMC free article] [PubMed] [Google Scholar]