By Harry Smith
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Additional resources for Commentaries in Plant Science
I I I . Comparison of the primary structures of the large and small subunits obtained f r o m five species of Nicotiana. Biochim. biophys. Acta 236 (1971) 578-586. K A W A S H I M A , N. G. Studies on Fraction I protein. IV. Mode of inheritance of primary structure in relation to whether chlorophyll or nuclear D N A contains the code for a chloroplast protein. Biochim. biophys. Acta 2 6 2 ( 1 9 7 2 ) 42-49. C. and M A T H E S O N , A. A simplified purification and some properties of ribulose 1,5-diphosphate carboxylase f r o m barley.
By all the methods tried. Fraction I protein is inseparable by incubating w i t h M g from RBP carboxylase, and meets the criteria for homogeneity. /mg. 0 and 3 0 ° C . Contaminating proteins of high 3 specific activity are thus easy to overlook, and may account for the oxygenase a c t i v i t y . T w o observations are consistent w i t h this; firstly, the ratio of oxygenase t o carboxylase activity increases two-fold during purification of the oxygenase, and secondly, the carboxylase loses two-thirds of its 3 activity during three weeks storage While the oxygenase activity remains constant .
0 and 3 0 ° C . Contaminating proteins of high 3 specific activity are thus easy to overlook, and may account for the oxygenase a c t i v i t y . T w o observations are consistent w i t h this; firstly, the ratio of oxygenase t o carboxylase activity increases two-fold during purification of the oxygenase, and secondly, the carboxylase loses two-thirds of its 3 activity during three weeks storage While the oxygenase activity remains constant . These observations do not prove that the oxygenase is a contaminant, since selective denaturation of distinct active sites may account for them, but it is clear that more evidence is needed t o confirm that the oxygenase activity is a property of Fraction I protein.