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J Bacteriol. 1965 December; 90(6): 1569-1574
Copyright © 1965 American Society for Microbiology. All Rights Reserved.

Incorporation of C¹⁴ from Amino Acids and Peptides into Protein by Clostridium perfringens Type D

Connaught Medical Research Laboratories, University of Toronto, Toronto, Ontario, Canada

ABSTRACT

HAUSCHILD, ANDREAS H. W. (University of Toronto, Toronto, Ontario, Canada). Incorporation of C¹⁴ from amino acids and peptides into protein by Clostridium perfringens type D. J. Bacteriol. 90:1569–1574. 1965.—Uptake of C¹⁴ from C¹⁴-labeled amino acids and peptides by Clostridium perfringens was measured in culture media containing acid or papain hydrolysates of C¹⁴-labeled Chlorella protein. Between 2 and 4 hr of growth, the rate of C¹⁴ uptake from peptides was higher than from free amino acids. Peptides extracted from cells with hot ethyl alcohol contained six to nine times more C¹⁴ after 4 hr of growth with C¹⁴-labeled peptides than with C¹⁴-labeled amino acids. Incorporation of C¹⁴-labeled glycine, serine, threonine, alanine, and proline into both cellular and exocellular protein was two to five times higher when these were supplied as components of dialyzable peptides rather than as free amino acids.