A comparison of the properties of 5'-nucleotidase purified from the cytosolic and synaptic plasma membrane fractions of rat forebrain.
1. 5'-Nucleotidase was purified 1247-fold from the post-microsomal supernatant (I) and 3862-fold from the synaptic plasma membrane (II) of rat brain homogenates. 2. The apparent molecular masses of I and II were 131 and 72 kDa respectively by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulphate and 268 and 286 kDa respectively by Sephacryl S-300 chromatography. 3. The activities of both I and II were strongly inhibited by concanavalin A but were affected differently by digestion with glycosidases. for II, these were 0.083 and 0.056 mM respectively. 5. Activities of both I and II were strongly inhibited by ATP and ADP.
Lai
K M
KM
Department of Biochemistry, Faculty of Medicine, University of Hong Kong.
Wong
P C
PC
D015720:5'-Nucleotidase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002412:Cations; D003600:Cytosol / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases / Q000378:metabolism; D007700:Kinetics; D037102:Lectins; D016548:Prosencephalon / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains; D013570:Synaptic Membranes / Q000201:enzymology*
D002412:Cations; D037102:Lectins; D015720:5'-Nucleotidase; D006026:Glycoside Hydrolases