Abstract: With a prerequisite of 5 hours in the light the detached leaves of wheat seedling and detached leaves and cotyledons of sunflower were able to utilize exogenous γ-aminobutyric acid, the amount of alanine and glutamine formed were increased. It was found that deamination of γ-aminobutyric acid was associated with γ-aminobutyric-pyruvate transaminase in the leaves of wheat seedling. The specific activity of this transaminase was enhanced about 5.6 fold by adsorption with calcium phosphate gel-Some properties of this transaminas were as follows: the optimum pH was 8.9. The produced amount of alanine was linear with time up to a period of one hour. The primary rate of reaction was proportional to enzyme concentration in the first hour. The relation of substrate concentration to the primary rate of alanine formation was determinated and Michaelis constant was evaluated about 2.6 × 10-3 M. The action of this transaminase in metabolism of γ-aminobutyrie acid was discussed.