Add time:09/26/2019         Source:sciencedirect.com

Publisher SummaryThis chapter describes the assay method, purification procedure, and properties of N5-formyltetrahydrofolic acid glutamic acid transformylase from hog liver. The method is based on the measurement of the tetrahydrofolic acid formed. The assay employed for tetrahydrofolic acid depend on the quantitative conversion of this compound into p-amino-benzoylglutamic acid in the Bratton-Marshall test for arylamines. Ascorbic acid and other reducing agents also interfere. The purified enzyme preparation contains formiminoglutamic acid formimino-transferase activity. In this connection, the purified formimino-transferase preparations contain transformylase activity. The hog liver transformylase appears to be distinct from the Pseudomonas formylglutamic acid formylase. No requirement for a folic acid derivative in the Pseudomonas system has been demonstrated. N10-Formylfolic acid, N10-formyltetrahydrofolic acid, and 5,10- methenyl-tetrahydrofolic acid are inactive. D-Glutamic acid and nineteen commonly occurring amino acids are inactive as acceptors. The reaction proceeds at one-fourth the rate if glutamine or isoglutamine replaces glutamic acid.

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