BIOLOGY OF LIGHT PRODUCTION — MALTJF 



393 



aqueous solutions of luciferin, even if luciferase is also present, will not luminesce 

 at this temperature. It is possible that in alcohol the oxidation proceeds at the 

 surface of luciferase particles, which pass the filter paper, suspended in the liquid. 

 The luminescence is not to be compared in brightness with that in aqueous solu- 

 tions with luciferase, and I mention these results merely as a matter of record, as 

 the only cases where Cypridina luciferin alone will luminesce. I do not believe 

 they are necessarily significant for the theory of bioluminescence because so many 

 organic substances luminesce on oxidation with strong oxidizing agents (Harvey, 

 1928). 



Various plants contain substances which, when added even to a 

 minute concentration of pyrogallol (even 1: 254,000) -f-H 2 2 yield 

 light (Harvey, 1916e). These substances are probably certain vege- 

 table peroxidases. 



If one mixes a test tube containing pyrogallol solution + hydrogen peroxide with 

 potato or turnip juice or almost any plant extract, a yellowish luminescence 

 appears. The plant extract loses the power to cause such luminescence on 

 boiling and the peroxidaze will not dialyze. It is, of course, comparable to 

 luciferase and acts on the thermostable, dialyzable pyrogallol-hydrogen peroxide 

 mixture, which is comparable to luciferin .... Although many hydroxy-phenol 

 and amino-phenol compounds can be oxidized by peroxidase and hydrogen 

 peroxide, only pyrogallol and gallic acid will oxidize with light production (Harvey). 



Table 1 . — Properties of luciferase and luciferin 



Property 



Salting out: 



Saturation with NaCl 



Yi saturation with (NHOsSOi. . . 



Saturation with (NH«) 2 S04 



Solubility: 



Ethyl alcohol 90 percent 



Ethyl alcohol 70 percent- 



Ethyl alcohol 50 percent 



Acetone 90 percent 



Ether 



Chloroform 



Xylol 



Alkaloidal reagents: 



Phosphotungstic acid 



Picric acid 



Heavy metal salts: 



Basic lead acetate 



Acids and alkalis: 



NaOH 



Trichloracetic acid 



HC1, after 16 hours boiling 



Heat: 



60° C 



Boiling 



Boiling with 4 percent HjSOi for 



10 hours. 

 Boiling for 24 hours with 4 per- 

 cent HjSOi. 

 Enzyme action: 



Trypsin, erepsin, amylase, 

 urease, sucrase, pepsinase, 

 rennin. 



Biuret reaction 



Dialysis 



Immunological (Harvey and Deit- 

 rick, 1930) . 



Luciferase 



Not precipitated 



Slightly precipitated 



Completely precipitated. 



Insoluble 



do 



Slightly soluble. 



Insoluble 



do 



do. 



do 



Completely precipitated. 



Nearly precipitated 



Completely precipitated.. 



Not precipitated. 



do 



Destroyed 



Irreversibly destroyed. 



do 



Destroyed 



.do. 



Destroyed only by pepsin (?), by 

 trypsin, erepsin, and something 

 in spleen and liver extracts. 



Positive 



Will not dialyse through celloidin.. 



Produces an antibody 



Luciferin 

 (more simple than luciferase) 



Not precipitated. 



Do. 

 Nearly completely precipitated. 



Soluble. 



Do. 



Do. 



Do. 

 Insoluble. 



Do. 



Do. 



Very nearly completely precip- 

 itated. 

 Not precipitated. 



Not completely precipitated. 



Not precipitated. 



Do. 

 Hydrolysed. 



Not destroyed. 

 Do. 

 Do. 



Destroyed. 



Not destroyed. 



Negative. 



Will dialyse through celloidin. 



Does not produce an antibody. 



Table 1 represents a summary of the most important data disclosed 

 by Harvey with regard to the properties of the luciferin and luciferase 



