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| http://purl.uniprot.org/citations/3119584 | http://www.w3.org/2000/01/rdf-schema#comment | "The primase associated with the DNA polymerase-primase of Drosophila melanogaster fails to show enzymatic turnover. However, it does show turnover when dissociated from the intact polymerase-primase. Both forms of the enzyme can catalyze the synthesis of primers that are not complementary to the DNA template. Like the intact enzyme, the isolated primase synthesizes primers of a unique chain length; however, they are twice as long as those synthesized by the polymerase-primase. The activity of the primase separated from the polymerase-primase is similar in all other respects to the intact polymerase-primase."xsd:string |
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| http://purl.uniprot.org/citations/3119584 | http://purl.uniprot.org/core/author | "Lehman I.R."xsd:string |
| http://purl.uniprot.org/citations/3119584 | http://purl.uniprot.org/core/author | "Cotterill S."xsd:string |
| http://purl.uniprot.org/citations/3119584 | http://purl.uniprot.org/core/author | "Chui G."xsd:string |
| http://purl.uniprot.org/citations/3119584 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/3119584 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
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| http://purl.uniprot.org/citations/3119584 | http://purl.uniprot.org/core/title | "DNA polymerase-primase from embryos of Drosophila melanogaster. DNA primase subunits."xsd:string |
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