CHAIRMAN S INTRODUCTION 579 



biochemistry from low molecular weight intermediates to macromolecule 

 biosynthesis and even to the structure, function, and synthesis of what 

 might be thought the deepest secret of biology — the gene. But with mem- 

 branes function is even more intimately related to structure. When one 

 tries the usual biochemical approach of first chopping the material up, 

 normal function, which requires separation of two aqueous phases by the 

 membrane, disappears. Here, more than in most of cell physiology, Goethe's 

 awed attitude toward Nature still applies : 



Und was sie deinem (ieist nicht oftenbaren mag, 



Das zwingst du ihr nicht ab mit Hebeln und mit Schrauben. 



Nevertheless, it is clear that I have exaggerated for rhetorical purposes. 

 Certain fruitful approaches to various aspects of the problem will be 

 described by this morning's participants, and Dr. Holter has already 

 introduced the phenomenon of pinocytosis. Among other recent en- 

 couraging biochemical developments, not represented here, it has been 

 observed that stimulation of the activity of secretory glands is associated 

 with increased phospholipid turnover [i8]; and from erythrocyte mem- 

 branes there has been separated an ATPase that is activated bv K+ plus 

 Na+ [19]. Finally, since the formation of specific transport systems in 

 bacteria is readily subject to experimental control, there are as yet un- 

 exploited possibilities for comparing directly the properties of two 

 membranes which should differ only with respect to a single system. In 

 complex problems of biology, as genetics has particularly shown, we can 

 learn a great deal from studying discrete differences in a single component 

 long before we have learned how to isolate it. 



References 



1. Gilvarg, C, and Davis, B. D.,J. biul. Chem. 222, 307 (1956). 



2. Davis, B. D., //; "Enzymes: Units of Biological Structure and Function", ed. 

 O. H. Gaebler. Academic Press, New York, 509 (1956). 



3. Krebs, H. A., in "Symposium sur le Cycle Tricarboxylique, Deuxieme 

 Congres Internationale de Biochimie", Paris, 1952. 



4. Davis, B. D., Arch. Biochetn. Biophys. 78, 497 (1958). 



5. Gale, E. F.,jf. gen. Microbiol. I, 53 (1947); Bull. Johns Hopk. Hosp. 83, 119 

 (1948). 



6. Cohen, G. N., and Rickenberg, H. V., Ann. Inst. Pasteur 91, 693 (1956). 



7. Rickenberg, H. W., Cohen, G. X., Buttin, G., and Monod, J., Ann. Inst. 

 Pasteur 91, 829 (1956). 



8. Cohen, G. N., and Monod, J., Bact. Rev. 21, 169 (1957). 



9. Mathieson, AI. J., and Catcheside, D. G.,jf. gen. Microbiol. 13, 72 (i955)- 



10. Davis, B. D., and Weiss, U., Arch. e.xp. Path. Pharmak. 220, i (1953). 



11. Barrett, J. T., Larson, A. D., and Kallio, R. E..^. Bact. 65, 187 (1953). 



12. Kogut, M., and Podoski, E. P., Biochem.jf. 55, 800 (1953). 



13. Green, H., and Davis, B. D., cited in ref. [2]. 



