AFFINITY CHROMATOGRAPHY OF BRAIN GLUTAMATE DECARBOXYLASE (EC 4.1.1.15) USING IMMOBILIZED PYRIDOXAL PHOSPHATE

1978 ◽  
pp. 81-84
Author(s):  
Alfred Fleissner
Keyword(s):  
Affinity Chromatography ◽  
Glutamate Decarboxylase ◽  
Pyridoxal Phosphate

Seizure susceptibility in the developing mouse and its relationship to glutamate decarboxylase and pyridoxal phosphate in brain

1975 ◽  
Vol 6 (2) ◽  
pp. 159-170 ◽  
Author(s):  
Ricardo Tapia ◽  
Herminia Pasantes-Morales ◽  
Efrain Taborda ◽  
Miguel P�rez de la Mora
Keyword(s):  
Glutamate Decarboxylase ◽  
Pyridoxal Phosphate ◽  
Seizure Susceptibility

Modifications of brain glutamate decarboxylase activity by pyridoxal phosphate-γ-glutamyl hydrazone

1967 ◽  
Vol 16 (7) ◽  
pp. 1211-1218 ◽  
Author(s):  
Ricardo Tapia ◽  
Miguel Pérez De La Mora ◽  
Guillermo H. Massieu
Keyword(s):  
Glutamate Decarboxylase ◽  
Pyridoxal Phosphate ◽  
Decarboxylase Activity

Synthesis of affinity chromatography resins for the purification of brain glutamate decarboxylase

1977 ◽  
Vol 2 (1) ◽  
pp. 51-57 ◽  
Author(s):  
Lourival D. Possani ◽  
Alejandro Bay�n ◽  
Ricardo Tapia
Keyword(s):  
Affinity Chromatography ◽  
Glutamate Decarboxylase

scholarly journals Interaction of L-threo and L-erythro isomers of 3-fluoroglutamate with glutamate decarboxylase from Escherichia coli

1985 ◽  
Vol 229 (3) ◽  
pp. 675-678 ◽  
Author(s):  
A Vidal-Cros ◽  
M Gaudry ◽  
A Marquet
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Glutamate Decarboxylase ◽  
Fluorine Atom ◽  
Pyridoxal Phosphate ◽  
Succinic Semialdehyde ◽  
E Coli ◽  
Rigid Conformation ◽  
The Difference ◽  
Hydrolysis Of

L-threo-3-Fluoroglutamate and L-erythro-3-fluoroglutamate were tested with glutamate decarboxylase from Escherichia coli. Both isomers were substrates: the threo isomer was decarboxylated into optically active 4-amino-3-fluorobutyrate, whereas the erythro isomer lost the fluorine atom during the reaction, yielding succinic semialdehyde after hydrolysis of the unstable intermediate enamine. The difference between the two isomers demonstrates that the glutamic acid-pyridoxal phosphate Schiff base is present at the active site under a rigid conformation. Furthermore, although the erythro isomer lost the fluorine atom, yielding a reactive aminoacrylic acid in the active site, no irreversible inactivation of E. coli glutamate decarboxylase was observed.

Activation by adenosine-5′-triphosphate of glutamic decarboxylase from a subcellular fraction of mouse brain

1979 ◽  
Vol 57 (8) ◽  
pp. 873-877 ◽  
Author(s):  
Godfrey Tunnicliff ◽  
That T. Ngo
Keyword(s):  
Mouse Brain ◽  
Glutamate Decarboxylase ◽  
Subcellular Fraction ◽  
Pyridoxal Phosphate ◽  
Control Mechanism ◽  
Decarboxylase Activity

Glutamate decarboxylase from a mouse brain P2 fraction undergoes a twofold activation in the presence of 0.5 mM ATP. No such stimulation by ATP occurs if the enzyme is assayed in the presence of excess pyridoxal phosphate as cofactor. The ATP-induced stimulation is almost completely eliminated if the enzyme is dialysed before its assay. [γ-32P]ATP present during the enzyme measurement is converted to [32P]pyridoxal phosphate. These results demonstrate that the activation produced by ATP is the result of the generation of cofactor during the course of the assay. This phenomenon may be a reflection of a control mechanism of glutamate decarboxylase activity.

scholarly journals An examination of potential matrices for the affinity chromatography of NADP+-linked dehydrogenases with special reference to 6-phosphogluconate dehydrogenase

1977 ◽  
Vol 161 (3) ◽  
pp. 561-568 ◽  
Author(s):  
P Griffiths ◽  
A Houlton ◽  
M J Adams ◽  
M J Harvey ◽  
P D G Dean
Keyword(s):  
Affinity Chromatography ◽  
Large Scale ◽  
Pyridoxal Phosphate ◽  
Specific Activity ◽  
Systematic Investigation ◽  
Inorganic Pyrophosphate ◽  
Phosphogluconate Dehydrogenase ◽  
Sheep Liver ◽  
Effects Of Ph ◽  
Careful Manipulation

1. 6-phosphogluconate dehydrogenase from sheep liver has been purified 350-fold by affinity chromatography with a final specific activity of 18 micronmol of NADP+/reduced min per mg of protein and an overall yield of greater than 40%. 2. A systematic investigation of potential ligands has been carried out: these included 6-phosphogluconate and NADP+, pyridoxal phosphate and several immobilized nucleotides. The results indicate that NADP+ is the most suitable ligand for the purification of 6-phosphogluconate dehydrogenase. 3. The effects of pH and alternative eluents have been examined in relation to the parameters known to affect the desorption phase of affinity chromatography; careful manipulation of the elution conditions permitted the separation of glucose 6-phosphate dehydrogenase, glutathione reductase and 6-phosphogluconate dehydrogenase from sheep liver on NADP+-Sepharose 4B. 4. A large-scale purification scheme for 6-phosphogluconate dehydrogenase is presented that uses the competitive inhibitors inorganic pyrophosphate and citrate as specific eluents.

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