TRANSAMINATION 221 



Wyss (44) observed formation of considerable amounts of aspartic 

 acid when oxalacetic acid was added to crushed pea nodules. The 

 amount of aspartic acid found was somewhat greater when alanine 

 was also added. Whether the aspartic acid formation is due to 

 transamination or to some other reaction is not certain. 



Yeast and Bacteria.— Adler, Giinther, and Everett (45) reported 

 transaminase activity in yeast extracts. Adler et al. (46) state that 

 Bacterium coli {Escherichia coli) suspensions form oxalacetic acid 

 from alpha-ketoglutaric acid and aspartic acid, and that lactic acid 

 bacilli are capable of transamination, though at a slower rate than 

 Esch. coli. No experimental data are given in either of the above 

 papers. 



Experiments by the writer (63) showed that Lebedev juice pre- 

 pared from brewer's yeast was active in catalyzing the reaction 

 alpha-ketoglutaric acid plus Z(—) -aspartic acid, but not the reaction, 

 alpha-ketoglutaric acid plus Z(-f )-alanine. Baker's yeast showed no 

 activity with either system. Experiments with Esch. coli suspensions 

 (63) demonstrated that no transamination occurred between Z( + )- 

 glutamic acid and pyruvic acid, but did take place between 

 Z( + ) -glutamic acid and oxalacetic acid. Qt for the latter reaction 

 was 17.2. 



Transamination in uiuo. —Kritzmann (40) found that intravenous, 

 intramuscular,- or intraperitoneal injection of glutamic acid into 

 rabbits, pigeons, and white mice causes the rapid appearance of 

 alanine in the blood and the tissues. The pyruvic acid necessary 

 for this reaction is endogenous. The injection of alpha-ketoglutaric 

 acid plus alanine resulted in the formation of glutamic acid. No 

 transamination occurs in the blood itself. The failure of blood cells 

 to catalyze transamination has also been observed by the writer (63). 



Influence of Various Substances on Transamination 



Inhibitors.— None of the well-known inhibitors has any marked 

 effect on transamination with the exception of cyanide, which in 

 high concentrations (0.05 M) causes up to 80 per cent inhibition. 

 This is in all probability due to the formation of cyanohydrin. How- 

 ever, at 0.001 M concentration cyanide still causes an inhibition of 

 about 30 per cent, indicating that an effect on the enzyme system 

 may occur. Malonate, pyrophosphate, sodium fluoride, iodoacetate, 

 bromoacetate, arsenious oxide, and octyl alcohol have little or no 

 influence on transamination in pigeon breast muscle (10). 



With transaminase no inhibition of transamination between glu- 



