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.
journal_name
Neurochem Resjournal_title
Neurochemical researchauthors
Franco R,Canela EI,Bozal Jdoi
10.1007/BF00965016subject
Has Abstractpub_date
1986-03-01 00:00:00pages
423-35issue
3eissn
0364-3190issn
1573-6903journal_volume
11pub_type
杂志文章abstract::Systemic inflammation triggered by lipopolysaccharide (LPS) administration disrupts blood-brain barrier (BBB) homeostasis in animal models. This event leads to increased susceptibility of several encephalic structures to potential neurotoxicants present in the bloodstream. In this study, we investigated the effects of...
journal_title:Neurochemical research
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pub_type: 杂志文章,评审
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更新日期:1999-04-01 00:00:00
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更新日期:1996-11-01 00:00:00
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pub_type: 杂志文章,评审
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更新日期:2011-07-01 00:00:00
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