350 MAHLON B. HOAGLAND 



the literature will be found particularly in the reviews of Brachet / Borsook, 2 

 and Loft field, 7 which deal mostly with animal systems; and in the review 

 of Spiegelman 4 which is concerned mainly with bacterial systems. The 

 review of Chantrenne 8 covers both areas and is the most recent. Amino 

 acid activation, and attachment of amino acids to soluble RNA are em- 

 phasized in the papers of Novelli and DeMoss, 3 and of Hoagland, 14 and 

 in the symposium. 13 Recent developments in the physicochemistry of the 

 ribosomes is covered in the book "Microsomal Particles and Protein Syn- 

 thesis." 16 The review by Bonner 12 is chiefly concerned with plant studies, 

 and that of Campbell 11 relates to the biochemistry of cancer. The discus- 

 sions of Dalgliesh, 9 Monod, 10 and Crick 6 stress theoretical aspects of RNA 

 and protein synthesis). This phenomenon gives the author a degree of free- 

 dom and a degree of bondage: he may limit the scope of this treatise with 

 assurance that aspects of secondary interest to his aim will be well covered 

 elsewhere, but he is hard pressed to avoid saying that which has been said 

 better elsewhere. This paper will be limited to a consideration of recent 

 investigations in cell-free systems, particularly those derived from mam- 

 malian tissues which bear directly on the role of nucleic acid in protein 

 synthesis. The reader is referred to the reviews cited for details of earlier 

 work, and particularly to the complementary Chapter 38 by Gros concerned 

 with studies on protein synthesis in intact cellular systems, primarily bac- 

 terial. 



Much of what will be said hereafter, about the role of cellular RNA- 

 containing fractions in protein synthesis, will be predicated on the assump- 

 tion that the systems used do in fact measure protein synthesis. Therefore, 

 before proceeding further, it would be well to outline briefly the limitations 



4 S. Spiegelman, in "The Chemical Basis of Heredity" (W. D. McElroy and B- 



Glass, eds.), p. 232. Johns Hopkins Press, Baltimore, 1957. 

 * J. L. Simkin and T. S. Work, Nature 179, 1214 (1957). 



6 F. H. C. Crick, Symposia Soc. Expll. Biol. 12, 138 (1958). 



7 R. B. Loftfield, Progr. in Biophys. and Biophys. ('hem. 8, 347 (1957). 



8 H. Chantrenne, Ann. Revs. Biochem. 27, 35 (1958). 



9 C. E. Dalgliesh, Rec. trav. chim. 77, 634 (1958). 



10 J. Monod, Rec. trav. chim. 77, 569 (1958). 



11 P. N. Campbell, Advances in Cancer Research 5, 97 (1958). 



12 J. Bonner, Fortschr. Chem. org. Naturstoffe 16, 139 (1958). 



13 Symposium on Amino Acid Activation, Proc. Sail. Acad. Sci. U. S. 44, 67 (1958). 



14 M. B. Hoagland, Proc. 4th Intern. Congr. Biochem., Vienna, 1958. 



15 I. 1). Raacke, Quart. Rev. Biol. 33, 245 (1958). 



16 "Microsomal Particles and Protein Synthesis" (R. B. Roberts, ed.). Pergamon, 

 London, 1958. (a) G. E. Palade, p. 36; (b) M. L. Petermann el al., p. 70; (c) J. K. 

 Ashikawa, p. 76; (d) R. B. Roberts et al., p. 84; (e) S. Dagley and J. Sykes, p. 62; 

 (f) J. Wagman and W. Trawick, p. 11; (g) W. C. Gillchriest and R. M. Bock, p. 1; 

 (h) B. D. Hall and P. Doty, p. 27; (i) H. Dintzis et al.. p. 93. 



