Mouse mammary carcinoma delta-aminolevulinate dehydratase

Comp Biochem Physiol B. 1990;96(4):729-31. doi: 10.1016/0305-0491(90)90221-e.

Abstract

1. Aminolevulinate dehydratase (ALA-D) was studied in crude extract from mouse mammary carcinoma, normal mouse liver and tumour bearing mouse liver. 2. A Michaelis-Menten behaviour and Km values between 0.24 and 0.31 mM were obtained for the enzyme in either source. 3. In all three tissues there was a linear relationship between porphobilinogen formation and incubation time, up to 120 min, ALA-D was thermostable and optimum pH was at 6.8. 4. There seems to be no structural alterations in tumoural ALA-D as compared with the enzyme from liver of both normal and tumour bearing mice.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Enzyme Stability
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Kinetics
  • Liver / enzymology
  • Male
  • Mammary Neoplasms, Experimental / enzymology*
  • Mice
  • Mice, Inbred BALB C
  • Porphobilinogen / metabolism
  • Porphobilinogen Synthase / metabolism*

Substances

  • Porphobilinogen
  • Porphobilinogen Synthase