Phosphorylase purine nucleoside
Phosphorylase purine nucleoside structure
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Common Name | Phosphorylase purine nucleoside | ||
|---|---|---|---|---|
| CAS Number | 9030-21-1 | Molecular Weight | 143.574 | |
| Density | 1.4±0.1 g/cm3 | Boiling Point | 409.3±40.0 °C at 760 mmHg | |
| Molecular Formula | C5H6ClN3 | Melting Point | N/A | |
| MSDS | USA | Flash Point | 201.3±27.3 °C | |
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Initial characterization of the human central proteome.
BMC Syst. Biol. 5 , 17, (2011) On the basis of large proteomics datasets measured from seven human cell lines we consider their intersection as an approximation of the human central proteome, which is the set of proteins ubiquitously expressed in all human cells. Composition and properties... |
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Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet. 36 , 40-5, (2004) As a base for human transcriptome and functional genomics, we created the "full-length long Japan" (FLJ) collection of sequenced human cDNAs. We determined the entire sequence of 21,243 selected clones and found that 14,490 cDNAs (10,897 clusters) were unique... |
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res. 14 , 2121-7, (2004) The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a r... |
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Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem. 81(11) , 4493-501, (2009) The analysis of proteome-wide phosphorylation events is still a major analytical challenge because of the enormous complexity of protein phosphorylation networks. In this work, we evaluate the complementarity of Lys-N, Lys-C, and trypsin with regard to their ... |
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[Influence of ionizing radiation on enzymatic activity and state of nucleus-nucleolar apparatus in rat hepatocytes].
Radiats. Biol. Radioecol. 53(1) , 55-62, (2013) The effects of a single exposure of rats to the whole-body roentgen irradiation at the doses of 3.5 Gy and 4.5 Gy on the activity of creatine kinase, purine nucleoside phosphorylase, alanine aminotransferase, aspartate aminotransferase, as well as on the stat... |
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Thermodynamic analysis of transition-state features in picomolar inhibitors of human 5'-methylthioadenosine phosphorylase.
Biochemistry 52(46) , 8313-22, (2013) Human 5'-methylthioadenosine phosphorylase (MTAP) is solely responsible for 5'-methylthioadenosine (MTA) metabolism to permit S-adenosylmethionine salvage. Transition-state (TS) analogues of MTAP are in development as anticancer candidates. TS analogues of MT... |
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DNA sequence and analysis of human chromosome 9.
Nature 429(6990) , 369-74, (2004) Chromosome 9 is highly structurally polymorphic. It contains the largest autosomal block of heterochromatin, which is heteromorphic in 6-8% of humans, whereas pericentric inversions occur in more than 1% of the population. The finished euchromatic sequence of... |
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Continuous enzyme-coupled assay of phosphate- or pyrophosphate-releasing enzymes.
Biotechniques 53(2) , 99-103, (2012) A coupled enzyme assay able to monitor the kinetics of reactions catalyzed by phosphate- or pyrophosphate-releasing enzymes is presented here. The assay is based on the concerted action of inorganic pyrophosphatase (PPase), purine nucleoside phosphorylase (PN... |
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Trimeric purine nucleoside phosphorylase: exploring postulated one-third-of-the-sites binding in the transition state.
Bioorg. Med. Chem. 20(22) , 6758-69, (2012) Transition-state analogue inhibitors, immucillins, were reported to bind to trimeric purine nucleoside phosphorylase (PNP) with the stoichiometry of one molecule per enzyme trimer [Miles, R. W.; Tyler, P. C.; Furneaux, R. H.; Bagdassarian, C. K.; Schramm, V. ... |
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A continuous kinetic assay for adenylation enzyme activity and inhibition.
Anal. Biochem. 404 , 56-63, (2010) Adenylation/adenylate-forming enzymes catalyze the activation of a carboxylic acid at the expense of ATP to form an acyl-adenylate intermediate and pyrophosphate (PP(i)). In a second half-reaction, adenylation enzymes catalyze the transfer of the acyl moiety ... |