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dc.contributor.authorGuy, G.R.
dc.contributor.authorDaniel, Roy M.
dc.date.accessioned2010-09-02T04:54:13Z
dc.date.available2010-09-02T04:54:13Z
dc.date.issued1982
dc.identifier.citationGuy, 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.en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4515
dc.description.abstractA 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.en_NZ
dc.language.isoen
dc.relation.urihttp://www.biochemj.org/bj/203/bj2030787.htmen_NZ
dc.subjectbiologyen_NZ
dc.titleThe purification and some properties of a stereospecific D-asparaginase from an extremely thermophilic bacterium, Thermus aquaticus.en_NZ
dc.typeJournal Articleen_NZ


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