The presence and orientation of ecto-5'-nucleotidase in rat liver lysosomes.
Purified rat liver lysosomes contained 5'-nucleotidase activity which was 92 +/- 2% [4]latent. This latency was lost in response to a permeant sugar at a similar rate to that of the lysosomal marker enzyme beta-N-acetylglucosaminidase indicating that the 5'-nucleotidase was genuinely located in the lysosome and not a plasma membrane contaminant. Lysosomal 5'-nucleotidase exhibited the following properties characteristic of ecto-5'-nucleotidase inhibition by specific polyclonal antibodies: binding to a monoclonal antibody; inhibition by 1 mmol/1 alpha beta-methylene ADP; immunoreactive subunits of 70 and 38 kDa. Lysosomes in addition contained immunoreactive species of intermediate molecular mass.
Maguire
G A
GA
Luzio
J P
JP
D015720:5'-Nucleotidase; D000818:Animals; D007163:Immunosorbent Techniques; D008099:Liver / Q000648:ultrastructure*; D008247:Lysosomes / Q000201:enzymology*; D051379:Mice; D008970:Molecular Weight; D009708:Nucleotidases / Q000032:analysis*; D011487:Protein Conformation; D051381:Rats
D009708:Nucleotidases; D015720:5'-Nucleotidase