Purification of the glutamate decarboxylase from human brain]

A method of purifying the glutamate decarboxylase from human brain is described. The enzyme was purified 8 000 fold in regard to the initial homogenate and appears homogenous by electrophoresis, both in denaturing and non-denaturing conditions. The molecular weight of the native enzyme and its subunits indicate that GAD from human brain is formed by two similar if non identical polypeptide chains. The Km for glutamate and pyridoxal phosphate found for the human enzyme, respectively 1,2.10(-3) M and 0,13.10(-6) M, are close to the Km found for the Mouse enzyme.     

Glutamate decarboxylase activity in brain regions of differentially-housed mice; a difference in the olfactory bulb

Summary Glutamate decarboxylase (GAD) activities were determined in homogenates of 8 brain regions of mice that had been differentially housed (isolated vs grouped) for 4–9 weeks. GAD activity was lower in whole forebrains and in olfactory bulbs of isolated mice, changes which might be associated with their increased aggressiveness.