title: Heterogeneous localization of some purine enzymes in subcellular fractions of rat brain and cerebellum.
abstract: The activity of guanine deaminase (GAH, E.C.3.5.4.3) was lower in rat cerebellum soluble and microsomal fractions than in rat brain subfractions. Adenosine deaminase (ADA, E.C.3.5.4.4) activity was released in higher proportion than guanine deaminase, purine nucleoside phosphorylase (PNP, E.C.2.1.2.4), 5'-nucleotidase (5'N, E.C.3.1.3.5), and lactate (LDH, E.C. 1.1.1.27) and malate (MDH, E.C. 1.1.1.37) dehydrogenase in press-juices of rat brain. Furthermore, nerve ending-derived fractions (synaptosomes and synaptic vesicles) showed an enrichment of adenosine deaminase and also of 5'-nucleotidase. The action of deoxycholate over the subfractions did not increase the activity of either enzyme. The contrary occurred with the remaining enzymes studied. Thus, it is possible that one set of enzymes are located on the surface of the particulate vesicles, whereas another set are located inside these vesicles, suggesting a compartmentation of purine catabolic enzymes in different areas of the central nervous system.
mesh_terms: D015720:5'-Nucleotidase; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002237:Carbohydrate Dehydrogenases / Q000378:metabolism; D002531:Cerebellum / Q000201:enzymology*; D008297:Male; D008854:Microscopy, Electron; D008861:Microsomes / Q000201:enzymology / Q000648:ultrastructure; D009708:Nucleotidases / Q000378:metabolism; D009709:Nucleotide Deaminases / Q000378:metabolism; D011683:Purine-Nucleoside Phosphorylase / Q000378:metabolism; D011687:Purines / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013347:Subcellular Fractions / Q000201:enzymology; D013572:Synaptic Vesicles / Q000201:enzymology / Q000648:ultrastructure; D013574:Synaptosomes / Q000201:enzymology / Q000648:ultrastructure
chemical_list: D011687:Purines; D002237:Carbohydrate Dehydrogenases; D011683:Purine-Nucleoside Phosphorylase; D009708:Nucleotidases; D015720:5'-Nucleotidase; D009709:Nucleotide Deaminases