Abstract
The polypeptides of the proteolytic rumen bacteriumBacteroides ruminicola R8/4 grown in the presence of either leaf Fraction 1 protein, bovine serum albumin, or Bactocasitone as sole nitrogen source were separated by SDS-polyacrylamide gel electrophoresis. Over 40 polypeptides were resolved; the pattern for organisms grown on Fraction 1 protein was similar but not identical to that of the serum albumin and Bactocasitone-grown bacteria. All the bacterial polypeptides were distinguishable from the polypeptides of Fraction 1 protein (and serum albumin). The stained pattern was the same for organisms sampled at intervals during the growth of a batch culture. After incubation of the growing organisms with [14C]-Fraction 1 protein, all the bacterial polypeptides were labeled.
Bacteria grown in the presence of nonlabeled Fraction 1 protein and a mixture of [14C]-labeled amino acids incorporated label into all the polypeptides; the bacteria did not grow in the absence of intact protein, and then virtually no label was incorporated from the amino acid mixture.
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Munn, E.A., Hazlewood, G.P. & Graham, M. Uptake and incorporation of the products of proteolysis by the rumen bacteriumBacteroides ruminicola R8/4. Current Microbiology 8, 317–320 (1983). https://doi.org/10.1007/BF01573701
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DOI: https://doi.org/10.1007/BF01573701