Purification and some properties of the soluble and membrane-bound adenosine deaminases of Micrococcus sodonensis ATCC 11880 and their distribution within the family Micrococcacea

Can J Biochem. 1975 Mar;53(3):344-53. doi: 10.1139/o75-048.

Abstract

In Micrococcus sodonensis and some other Micrococcus species, adenosien deaminase is present both as a membran-bound and a soluble enzyme; The membran-bound adenosine deaminase can be extracted with n-butanol, and may account for up to 5% of the total cellular adenosine deaminase activity. In a number oc comparative tests, no differences between the two enzyme forms could be found, thus they are believed to be similar molecular species; The purified membran-bound or soluble enzyme had a molecular weight, obtained by gel-filtration, of 130 000 and was inactive toward adenine and adenine mononucleotides. It appears, therefore, to be more closely related to the calf-intestine enzyme than the Aspergillus oryzae form in respect to size and substrate specificity; Attempts to correlate membrane-bound adenosine deaminase activity with adenosine transport in isolated membrane vesicles of M. sodonensis indicated no obvious relationship between the two activities.

MeSH terms

  • Adenosine / metabolism
  • Aminohydrolases / isolation & purification
  • Aminohydrolases / metabolism*
  • Animals
  • Antigen-Antibody Reactions
  • Biological Transport
  • Cell Membrane / enzymology
  • Chromatography, DEAE-Cellulose
  • Chromatography, Gel
  • Kinetics
  • Magnesium / pharmacology
  • Micrococcus / enzymology*
  • Micrococcus / metabolism
  • Molecular Weight
  • Rabbits / immunology
  • Solubility
  • Species Specificity
  • Spheroplasts / enzymology

Substances

  • Aminohydrolases
  • Magnesium
  • Adenosine