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      The purification and some properties of a stereospecific D-asparaginase from an extremely thermophilic bacterium, Thermus aquaticus.

      Guy, G.R.; Daniel, Roy M.
      Link
       www.biochemj.org
      Citation
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      Guy, G.R., Daniel, R.M. (1982). The purification and some properties of a stereospecific D-asparaginase from an extremely thermophilic bacterium, Thermus aquaticus. Biochemical Journal, 203, 787-790.
      Permanent Research Commons link: https://hdl.handle.net/10289/4515
      Abstract
      A specific D-asparaginase was isolated and crystallized from Thermus aquaticus strain T351. It is present in larger amounts than the L-asparaginase. The enzyme has a molecular weight of 60 000, an isoelectric point of 4.8 and a Km of 2 mM. It has 6 disulphide bonds/molecule, and a histidine residue at the active site. It is inhibited by keto acids and by high salt concentrations.
      Date
      1982
      Type
      Journal Article
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      • Science and Engineering Papers [3077]
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