This study is concerned with the metabolism of L-asparagine in Lactobacillus plantarum (ATCC 8014). Theprimary area of investigation is the preliminary characterization of a previously unreported L-asparaginase enzyme in L. plantarum. This L-asparaginase was determined to be an inducible enzyme with variations in its activity level according to the L-asparagine level in the growth medium. L-Glutaminase could not be induced in this organism by L-glutamine, nor would L-glutamine induce the asparaginase activity. These and other studies with amino acid analogs demonstrated the high specificity of both induction and enzymic activity of the asparaginase. Various physical properties of the enzyme were studied. The enzyme was found to be inhibited by adenosine triphosphate (ATP). This inhibition appears to be cooperative in nature and of the type exhibited by allosteric enzymes. These studies should be confirmed on a highly purified enzyme as these preliminary experiments were performed using a crude cell-free extract.
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc663794 |
| Date | 05 1900 |
| Creators | McCue, Bette Ann |
| Contributors | Norton, S. J., Skinner, Charles Gordon |
| Publisher | North Texas State University |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | vi, 59 leaves: ill., Text |
| Rights | Public, McCue, Bette Ann, Copyright, Copyright is held by the author, unless otherwise noted. All rights |
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