Rabbit Liver Guanine Deaminase
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چکیده
منابع مشابه
Rabbit Liver Guanine Deaminase
Homogeneous guanine deaminase (guanine aminohydrolase, EC 3.5.4.3) is a single polypeptide chain of mean molecular weight of 55,000, as determined by Sephadex gel filtration and sodium dodecyl sulfate polyacrylamide disc gel electrophoresis. Irreversible inactivation was observed upon incubation with P-chloromercuribenzoate, at a concentration of 1.0 x lop4 M. Iodoacetic acid and iodoacetamide ...
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1. Guanine deaminase in rat brain and liver was distributed among all the subcellular fractions: nuclei, ;heavy' mitochondria, ;light' mitochondria, microsomes and the supernatant fluid. The greater part of the activity passed into the soluble fraction. Among the particulate components, the ;light' mitochondria constituted the richest fraction. 2. The sum of the enzymic activities of the compon...
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Ontogeny of trimeric GTP-binding regulatory proteins (G-proteins) and their subunits in rabbit liver during neonatal development was studied, by using bacterial-toxin-catalysed ADP-ribosylation of membrane proteins, immunoblot analysis to quantify the alpha-subunit (alpha s and alpha i) of stimulatory (Gs) and inhibitory (Gi) G-protein and the beta-subunit, and reconstitution assay with cyc- me...
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1. Guanine deaminase activities in homogenates and supernatant fractions of liver and brain of rat and mouse were elevated by administration of guanine to the animals. The maximum induction in mouse tissues occurred within 24h and in rat tissues within 48h. 2. Mitochondria of rat (but not mouse) liver and brain contain an inhibitor of supernatant guanine deaminase, and this was also increased b...
متن کاملIdentification, expression, and characterization of Escherichia coli guanine deaminase.
Using the human cDNA sequence corresponding to guanine deaminase, the Escherichia coli genome was scanned using the Basic Local Alignment Search Tool (BLAST), and a corresponding 439-residue open reading frame of unknown function was identified as having 36% identity to the human protein. The putative gene was amplified, subcloned into the pMAL-c2 vector, expressed, purified, and characterized ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42554-4