On the Origin of the Fore-protein 117 



H H H H 



C C 



-NH C — NH C — NH 



o o o o o 



— C HN C HN C 



\ / \ / \ 



c c 



H H H H 



H R H R 



/ \ / \ / 



— NH C — NH C — NH 



o o o o o 



— C HN C HN C 



c c 



R H R H 



Fig. I. 



If polyglycine adsorbed on a solid surface had the configuration as indicated 

 in the above figure, the plane including one carbon atom and two hydrogen 

 atoms of the methylene group must be perpendicular to the solid surface. The 

 reacting molecule must have come from outside, and, therefore, only one 

 hydrogen atom directed to outside must have reacted, giving rise to amino acid 

 residues of the same stereochemical configuration throughout one single peptide 

 chain. 



The vaUdity of the second step in the above hypothesis was tested in the 

 following model experiments, which were carried out by Hanafusa in my 

 laboratory. Aminoacetonitrile was prepared by the condensation of formalde- 

 hyde, ammonia and hydrogen cyanide and was obtained in the form of its hydro- 

 gen sulphate. This was mixed with 20 parts of kaolinite and heated at 130-135° 

 for 5 hours. The product was extracted with dilute sodium hydroxide solution. 

 The presence of glycylglycine and glycylglycylglycine in the extract was con- 

 firmed by paper and column chromatography. 



The present paper deals mainly with experiments concerning the last step in 

 the formation of the fore-protein, that is the introduction of side chains into 

 polyglycine structure. Polyglycine used in the present work was prepared not 

 from aminoacetonitrile but from glycine N-carboxyUc anhydride or from glycine 

 ester, by polycondensation with or without supporter. Polyglycine spread on 



