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| http://purl.uniprot.org/citations/238936 | http://www.w3.org/2000/01/rdf-schema#comment | "During recent studies conducted with suspensions of three strains of Saccharomyces cerevisiae, it was observed that ammonia was rapidly liberated when L-asparagine was added to the medium. Subsequent investigation has revealed that these strains of S. cerevisiae have an externally active asparaginase as well as an internally active one. The appearance of the external asparaginase is stimulated by nitrogen starvation, requires an available energy source, and is prevented by cycloheximide. The internal enzyme appears to be constitutive. The external activity is relatively insensitive to para-hydroxymercuribenzoate inhibition, whereas the internal activity is highly inhibited by this compound."xsd:string |
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| http://purl.uniprot.org/citations/238936 | http://purl.uniprot.org/core/author | "Dunlop P.C."xsd:string |
| http://purl.uniprot.org/citations/238936 | http://purl.uniprot.org/core/author | "Roon R.J."xsd:string |
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| http://purl.uniprot.org/citations/238936 | http://purl.uniprot.org/core/name | "J Bacteriol"xsd:string |
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| http://purl.uniprot.org/citations/238936 | http://purl.uniprot.org/core/title | "L-Asparaginase of Saccharomyces cerevisiae: an extracellular Enzyme."xsd:string |
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