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

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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.

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