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By Harry Smith

ISBN-10: 0080197590

ISBN-13: 9780080197593

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It appears that some chemical feature of the carboxylation of RBP has defied all evolutionary attempts t o produce a more effective catalyst. SYNTHESIS The existence of prokaryote-like 70S ribosomes in chloroplasts in amounts as high as 50% of 10 the total ribosomes in a l e a f has generated many attempts to determine their function in chloroplast 11 d e v e l o p m e n t . T w o methods have been used t o try t o determine the sites of synthesis of chloroplast proteins:1) 2) by supplying 70S ribosomal inhibitors to cells making chloroplasts, and determining which proteins are no longer synthesised.

Activation of CO2 fixation in isolated spinach chloroplasts. Biochim. biophys. Acta 234 (1971) 360-370. 27. G. A. Photosynthesis by isolated chloroplasts. Proc. natn. Acad. Sei. S. 56 (1966) 1095-1101. 28. K A W A S H I M A , N. Comparative studies on Fraction I protein f r o m spinach and tobacco leaves. PI. , Tokyo 10 (1969) 31-40. 29. K A W A S H I M A , N. Non-synchronous incorpora1 tion of ^ C 0 2 into amino acids of the two subunits of Fraction I protein. Biochem. biophys. Res. Commun. 38 (1970) 119-124.

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.

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Commentaries in Plant Science by Harry Smith


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