Incorporation of C14from Amino Acids and Peptides into Protein byClostridium perfringensType D
- 1 December 1965
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 90 (6), 1569-+
- https://doi.org/10.1128/jb.90.6.1569-1574.1965
Abstract
Uptake of C14 from C14-iabeled amino-acids and peptides by C. 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 iabeled 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.This publication has 18 references indexed in Scilit:
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