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J Bacteriol. 1969 March; 97(3): 1160-1164
Copyright © 1969 American Society for Microbiology. All Rights Reserved.

Separation of Folic Acid Reductase from Streptococcus faecium (ATCC 8043)1

Eugene L. Speck and Lewis F. Affronti

a Department of Microbiology, The George Washington University School of Medicine, Washington, D.C. 20005

ABSTRACT

A strain of Streptococcus faecium (ATCC 8043) which is highly resistant to the antifolic acid compound, amethopterin, was gently ruptured by exposing protoplasts of the organism to a hypotonic solution. The crude lysate resulting there-from was treated by various chemical and physical techniques designed to separate folic acid reductase from dihydrofolic acid reductase. In the process, the enzyme was purified approximately 160-fold; however, throughout the process, the enzyme preparation maintained the ability to reduce folic acid to tetrahydrofolic acid. Attempts to isolate mutants showing a deficiency in either folic acid reductase or dihydrofolic acid reductase were unsuccessful. Based on these results, it is concluded that folic acid is reduced to tetrahydrofolic acid by one enzyme in S. faecium (ATCC 8043). The crude lysate was also subjected to ultracentrifugation. An analysis of the supernatant fluid and the sediment indicated that the reductive activity is located in the soluble fraction of the cell.

FOOTNOTES

1 Work reported is part of a dissertation submitted by E. L. Speck to the faculty of the Graduate Council, The George Washington University, in partial fulfillment of the requirements for the Ph.D. degree.

J Bacteriol. 1969 March; 97(3): 1160-1164
Copyright © 1969 American Society for Microbiology. All Rights Reserved.





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