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[96] Plasma folic acid conjugase

Methods in Enzymology, ISSN: 0076-6879, Vol: 66, Issue: C, Page: 670-678
1980
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  • Citations
    8
    • Citation Indexes
      8

Article Description

This chapter discusses the plasma folic acid conjugase. The development of solid-phase synthesis of the poly-γ-glutamates of folic acid has made possible the preparation of specifically labeled radioactive substrates that can be used for the assay of conjugase activity. The extent of liberation of radioactive glutamic acid by enzyme action on a suitably labeled synthetic substrate gives a measure of the enzyme activity. The separation of unreacted substrate from the liberated radioactive glutamate can be done by adsorption on charcoal under conditions that do not permit the binding of glutamic acid. The optimal pH for the plasma conjugase activity is 4.5. The enzyme activity is proportional to the period of incubation up to 3 h. The addition of sulfhydryl compounds like glutathione (reduced), cysteine, and mercaptoethanol results in increased enzyme activity and ascorbic acid has no effect. This shows that plasma conjugase is a sulfhydryl enzyme. The molecular weight of human plasma conjugase has been shown to be 110,000 by sephadex gel chromatography.

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