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. 1977 Mar;129(3):1379–1386. doi: 10.1128/jb.129.3.1379-1386.1977

Purification and properties of L-glutaminase-L-asparaginase from Pseudomonas acidovorans.

L Davidson, D R Brear, P Wingard, J Hawkins, G B Kitto
PMCID: PMC235113  PMID: 845119

Abstract

An enzyme that catalyzes the hydrolysis of both glutamine and asparagine has been purified to homogeneity from extracts of Pseudomonas acidovorans. The enzyme having a ratio of glutaminase to asparaginase of 1.45:1.0 can be purified by a relatively simple procedure and is stable upon storage. The glutaminase-asparaginase has a relatively high affinity for L-asparagine (Km=1.5 X 10(-5) M) and L-glutamine (Km=2.2 X 10(-5) M) and has a molecular weight of approximately 156,000 the subunit molecular weight being approximately 39,000. Injections of the enzyme produced only slight increases in the survival time of C3H/HE mice carrying the asparagine-requiring 6C2HED Gardner lymphoma and of white Swiss mice carrying the glutamine-requiring Ehrlich lymphoma.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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