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. 1974 Jul;141(1):211–217. doi: 10.1042/bj1410211

Deoxycytidylate deaminase. Properties of the enzyme from cultured kidney cells of baby hamster

Hilary A Rolton 1,*, Hamish M Keir 1
PMCID: PMC1168068  PMID: 4455201

Abstract

dCMP deaminase was partially purified from BHK-21/C13 cells grown in culture. The molecular weight of the enzyme was estimated by gel filtration and gradient centrifugation to be 130000 and 115000 respectively. The enzyme had a pH optimum of 8.4. Its activity versus substrate concentration curve was sigmoid, the substrate concentration at half-maximal velocity being 4.4mm. dCTP activated the deaminase maximally at 40μm, gave a hyperbolic curve for activity versus dCMP concentration and a Km value for dCMP of 0.91mm. dCTP activation required the presence of Mg2+ or Mn2+ ions. dTTP inhibited the deaminase maximally at 15μm; the inhibition required the presence of Mg2+ or Mn2+ ions. The enzyme was very heat-labile but could be markedly stabilized by dCTP at 0.125mm and ethylene glycol at 20% (v/v).

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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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