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. 1970 Jun;118(1):135–141. doi: 10.1042/bj1180135

Purification and general properties of glutamate decarboxylase from Clostridium perfringens

I Cozzani 1, A Misuri 1, C Santoni 1
PMCID: PMC1179089  PMID: 4319539

Abstract

1. A seven-step procedure for preparing highly purified glutamate decarboxylase from Clostridium perfringens is described. 2. The homogeneity of the pure enzyme was established by sucrose-density-gradient centrifugation and starch-gel electrophoresis. 3. The isoelectric point of the pure enzyme is about pH4.5 and the molecular weight is 290000. 4. The pH optimum for activity is 4.7. The pure enzyme is specific for l-glutamate; β-hydroxyglutamate is decarboxylated at a lower rate. 5. Evidence is presented that each mol of enzyme contains 2mol of firmly bound pyridoxal 5-phosphate. 6. Resolution does not occur at acid pH; by dilution with neutral or alkaline buffers the enzyme is inactivated and the coenzyme is released. 7. Reconstitution of active enzyme was obtained by protecting the apoenzyme with thiol compounds.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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