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Plant Physiology 71:404-408 (1983)
© 1983 American Society of Plant Biologists

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Articles

Relationship between the Kinetic Properties and the Small Subunit Composition of Nicotiana Ribulose-1, 5-bisphosphate Carboxylase 1

L. R. Li, Verne A. Sisson2 and S. D. Kung

Department of Biological Sciences, University of Maryland Baltimore County, Catonsville, Maryland 21228, United States Department of Agriculture, Agricultural Research Service, Tobacco Laboratory, Beltsville, Maryland 20705

Genetic variability in the large and small subunits of ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBPCase) in several Nicotiana species has been characterized by isoelectric focusing patterns. This heritable variation provides an opportunity to examine the functional role of each of these subunits. In this study, specifically designed RuBPCase enzymes composed of identical large subunits but different small subunits were constructed in vivo by interspecific hybridization between the species N. sylvestris, N. tabacum, N. glauca, N. glutinosa, N. plumbaginifolia, and N. tomentosiformis. Small subunit polypeptides were combined to form a sequence of one, two, three, and four polypeptides with the large subunit of N. sylvestris. Kinetic properties of these hybrid enzymes were compared. No differences in the specific activity of either carboxylation or oxygenation nor in Km values for ribulose 1,5-bisphosphate, CO2, or O2 were detected among the RuBPCase enzymes from the various interspecific hybrids. Likewise, the ratio of carboxylation to oxygenation was constant.

2 Present address: United States Department of Agriculture, Agricultural Research Service, Tobacco Research Laboratory, Route 2, Box 16G, Oxford, NC 27565.

1 Supported by National Institutes of Health grant CM22746-01 and United States Department of Agriculture Cooperative Agreement 58-3204-0-157.






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Copyright © 1983 by the American Society of Plant Biologists