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P Gonnard

Publications and source records attributed to P Gonnard.

At least 37 records · Page 2Linked to original sources

Purification and properties of 4-aminobutyrate 2-ketoglutarate aminotransferase from pig liver.

4-Aminobutyrate-transaminase (4-aminobutyrate: 2-oxoglutarate amino-transferase, EC 2.6.1.19) from pig liver has been purified to electrophoretic homogeneity. It has a molecular weight of about 110 000 and is composed of two subunits of the same molecular weight but of different charges. Two forms of pig liver 4-aminobutyrate-transaminase were isolated by DEAE-cellulose chromatography and designated as 4-aminobutyrate-transaminase I and 4-aminobutyrate-transaminase II, corresponding to a cationic and anionic form. Some physical and kinetic properties of liver enzyme were compared to those of brain enzyme and no significant difference were found, except for their sedimentation coefficients and the charges of their subunits. The role of 4-aminobutyrate-transaminase in liver remains a matter of speculation, but could be related to a metabolic function.

4-Aminobutyrate Transaminase↗

The effect of electrical stimulation upon the activity of brain glutamate decarboxilase "in vitro".

Using the cytoplasmic soluble fraction from rat brain as a source of glutamate decarboxilase, its enzymatic activity was induced by electrical stimulation and determined by gas release. Modified Warburg's flasks were used for such determination. The limits of frequency and the use of sinusoidal waves were based on normal cerebral rhythms. At low frequencies, GAD activity is markedly enhanced (1-10 Hz, 2v, 500 muA). Activation of the enzyme may be due to distortion of the tertiary structure promoting thus an increased coupling between the substrate and the enzyme complex.

Animals↗