Uroporphyrinogen decarboxylase from mouse mammary carcinoma and liver of normal and tumor-bearing mouse

Comp Biochem Physiol B. 1992 May;102(1):87-92. doi: 10.1016/0305-0491(92)90277-x.

Abstract

1. URO-D was investigated in crude extracts from mouse mammary carcinoma, normal mouse (NM) liver and tumor-bearing mouse (TBM) liver. 2. URO-D from TBM liver and tumor appears to be more sensitive to increasing concentrations of UROgen than the NM liver enzyme. 3. In tumor the rate-limiting step seems to be the decarboxylation of the first carboxyl group, but this was not so clear for the NM and the TBM liver URO-D. 4. URO-D activity was enhanced when incubated at higher temperatures in the presence of its substrate, suggesting that UROgen might afford some protection of the enzyme against heat inactivation. 5. The optimum pH for all three sources is around 7.0.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Hydrogen-Ion Concentration
  • Kinetics
  • Liver / enzymology
  • Male
  • Mammary Neoplasms, Experimental / enzymology*
  • Mice
  • Mice, Inbred BALB C
  • Substrate Specificity
  • Temperature
  • Uroporphyrinogen Decarboxylase / metabolism*
  • Uroporphyrinogens

Substances

  • Uroporphyrinogens
  • Uroporphyrinogen Decarboxylase