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 β- N-acetyl-glucosaminidase indicating that the 5'-nucleotidase was genuinely located...

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Bibliographic Details
Published in:FEBS letters 1985-01, Vol.180 (1), p.122-126
Main Authors: Maguire, Gerald A., Luzio, J.Paul
Format: Article
Language:English
Subjects:
5'-Nucleotidase
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Immunosorbent Techniques
liver
Liver - ultrastructure
lysosomes
Lysosomes - enzymology
Mice
Molecular Weight
Nucleotidases - analysis
Protein Conformation
Rat liver lysosome 5'-Nucleotidase Membrane cycling
Rats
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Summary: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 β- N-acetyl-glucosaminidase 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 l αβ-methylene ADP; immunoreactive subunits of 70 and 38 kDa. Lysosomes in addition contained immunoreactive species of intermediate molecular mass.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)80244-1