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Incorporation of C14 from amino acids and peptides into protein by Clostridium perfringens type D
Insights
Clostridium perfringens type D incorporated C(14)-labeled amino acids and peptides into protein. Uptake was higher from peptides, showing greater incorporation into cellular and exocellular protein.
Area of Science:
- Microbiology
- Bacteriology
- Protein Synthesis
Background:
- Clostridium perfringens type D is a bacterium relevant in microbiology.
- Understanding nutrient assimilation in bacteria is crucial for studying their growth and metabolism.
Purpose of the Study:
- To investigate the differential incorporation of carbon-14 (C(14)) from amino acids and peptides into protein by Clostridium perfringens type D.
- To compare the uptake rates and incorporation efficiency of C(14)-labeled amino acids versus peptides.
Main Methods:
- Culturing Clostridium perfringens type D in media containing C(14)-labeled amino acids and peptides derived from Chlorella protein hydrolysates.
- Measuring the C(14) uptake from both sources over a 2-4 hour growth period.
- Extracting cellular protein using hot ethyl alcohol to quantify incorporated C(14).
Main Results:
- The rate of C(14) uptake from peptides was significantly higher than from free amino acids between 2 and 4 hours of growth.
- Cellular peptides contained six to nine times more C(14) after 4 hours when supplied as labeled peptides compared to labeled amino acids.
- Incorporation of specific C(14)-labeled amino acids (glycine, serine, threonine, alanine, proline) into both cellular and exocellular protein was 2-5 times higher when provided as part of dialyzable peptides.
Conclusions:
- Clostridium perfringens type D preferentially utilizes peptides over free amino acids for protein synthesis.
- Peptides serve as a more efficient source of amino acids for incorporation into both cellular and secreted proteins in this bacterium.
Abstract:
Hauschild, Andreas H. W. (University of Toronto, Toronto, Ontario, Canada). Incorporation of C(14) from amino acids and peptides into protein by Clostridium perfringens type D. J. Bacteriol. 90:1569-1574. 1965.-Uptake of C(14) from C(14)-labeled amino acids and peptides by Clostridium perfringens was measured in culture media containing acid or papain hydrolysates of C(14)-labeled Chlorella protein. Between 2 and 4 hr of growth, the rate of C(14) uptake from peptides was higher than from free amino acids. Peptides extracted from cells with hot ethyl alcohol contained six to nine times more C(14) after 4 hr of growth with C(14)-labeled peptides than with C(14)-labeled amino acids. Incorporation of C(14)-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.