Formation of Amino Acids etc. 145 



a-Aminosuccinaldehydic acid is the basic compound for the formation of 

 lysine (12), (13), (14), (23), (24) and (25), arginine (12), (13), (31), (32), (33) 

 and histidine (34), (35), (36), (37), (38). The formation of glutamic acid can 

 also be traced to this compound (12), (13) and (17), Interconversion of glutamic 

 acid and lysine, arginine and histidine [25] has been observed in living tissues 

 [16-19]. Serine on condensation with formaldehyde, (9) and (10), changes to 

 homoserine. 



On a different condensation with two molecules of formaldehyde, (40) and 

 (41), and subsequent oxidation and decarboxylation, (42) and (43), serine forms 

 threonine. In Neiirospora, homoserine has been observed to go to threonine by 

 Teas, Horowitz & Fhng [26]. It is quite probable that even in this, serine is an 

 intermediate compound. 



Thus the formation of a number of amino acids can be explained through 

 the intermediate formation of free radicals by making use of simple reactions as 

 condensation, oxidation, reduction, intermolecular changes etc. These can be 

 made to take place under laboratory conditions by using drastic reagents and 

 by keeping the thermodynamic level constant. Under the influence of light, 

 these reactions take place under normal conditions. 



The chain reactions initiated by light do not stop at the amino acid stage, 

 helping in the formation and dynamic interconversion of the amino acids as 

 observed by us [3] but continue, resulting in the formation of compounds with 

 peptide linkage. The different amino acids formed unite differently, forming 

 different types of peptides. Even though the possible number of such peptides 

 is very large, only a few stable ones remain in the mixture for an appreciable time 

 and the others soon hydrolyse to amino acids which recombine to give newer 

 peptides. The peptides can be of molecvdar weights of the order of protein, but 

 only a few such aggregates get a chance to remain stable imder the activated 

 state of the mixture and in most of them there will be a state of continuous mole- 

 cular change initiated by the irradiating electromagnetic waves. These are under 

 investigation in our laboratories. Considering the result of our experiments and 

 the work carried out on mitogenetic radiations [27] I have come to the following 

 conclusions on the problem of the origin of life. 



Consider a macromolecule formed by the activation of Hght. It is a huge 

 molecule of indefinite shape, of numerous peptide linkages and having various 

 groups attached to it and the molecule is in such a state that if activated or 

 excited by hght it can undergo a number of permutations and combinations with 

 Httle or no change in its thermodynamic energy level, resulting in the formation 

 of different protein molecules. This macromolecule is made by the imion of 

 different amino acids by the influence of hght. 



It is known that in a protein molecule, there are fluctuating electric charges 

 [28]. Hence in this macromolecular aggregate, also, there will be fluctuating 

 electric charges. Whenever there is a fluctuating charge, radiations of a mito- 

 genetic order are emitted. 



During the disintegration and synthesis of certain systems by electromagnetic 

 waves, A. & L. Gurwitsch have observed that if a 3% gelatinized nucleic acid 

 solution is irradiated with 3220-3240 Â wavelength radiation a secondary radi- 



