PMID:16751: Difference between revisions
New PMID: Page! |
imported>Wikientrybot change PMID template to TableEdit version |
||
| (7 intermediate revisions by 2 users not shown) | |||
| Line 1: | Line 1: | ||
{{RightTOC}} | {{RightTOC}} | ||
<!--box uid=d41d8cd98f00b204e9800998ecf8427e.130965.R52238d2d39496--> | |||
<!-- | |||
****************************************************************************************** | |||
* | |||
* ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | |||
* | |||
****************************************************************************************** --> | |||
{| id="R52238d2d39496" class=" tableEdit PMID_info_table" | |||
|- | |||
!align=left |Citation | |||
|| | |||
'''Leer, JC, Hammer-Jespersen, K and Schwartz, M''' (1977) Uridine phosphorylase from Escherichia coli. Physical and chemical characterization. ''Eur. J. Biochem.'' '''75''':217-24 | |||
|- | |||
!align=left |Abstract | |||
|| | |||
Uridine phosphorylase from Escherichia coli has been purified to homogeneity. The enzyme was found to have a molecular weight of 176000 and to consist of 8 probably identical subunits with molecular weights of 22000. These numbers were determined from equilibrium centrifugations in the analytical ultracentrifuge, from dodecylsulphate gel electrophoresis and from amino acid analysis. Moreover the following physico-chemical constants were determined: s020,w = 8.2 x 10(-13) s, upsilon2 = 0.751 cm3/g, A1%280 (1 cm) = 6.73 and a specific activity of 183 units/mg towards uridine. The enzyme shows some activity towards deoxyuridine and thymidine. The activity is not impaired through substitution by bromo, fluoro or methyl groups in the 5-position of the uracil base, but no enzymatic activity is observed when cytosine base is used in the nucleoside substrate. | |||
|- | |||
!align=left |Links | |||
|| | |||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16751 PubMed] | |||
|- | |- | ||
| | !align=left |Keywords | ||
|| | |||
|- | Amino Acids/analysis; Drug Stability; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; Pentosyltransferases/isolation & purification; Protein Conformation; Thymidine Phosphorylase/isolation & purification; Uridine Phosphorylase/isolation & purification; Uridine Phosphorylase/metabolism | ||
|{{ | |||
|- class="tableEdit_footer" | |||
|<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.130965.R52238d2d39496&page=130965&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> || | |||
|} | |} | ||
< | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.130965.R52238d2d39496--> | ||
==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
| Line 19: | Line 38: | ||
==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
< | <annotationlinks/> | ||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Latest revision as of 04:30, 15 September 2013
| Citation |
Leer, JC, Hammer-Jespersen, K and Schwartz, M (1977) Uridine phosphorylase from Escherichia coli. Physical and chemical characterization. Eur. J. Biochem. 75:217-24 |
|---|---|
| Abstract |
Uridine phosphorylase from Escherichia coli has been purified to homogeneity. The enzyme was found to have a molecular weight of 176000 and to consist of 8 probably identical subunits with molecular weights of 22000. These numbers were determined from equilibrium centrifugations in the analytical ultracentrifuge, from dodecylsulphate gel electrophoresis and from amino acid analysis. Moreover the following physico-chemical constants were determined: s020,w = 8.2 x 10(-13) s, upsilon2 = 0.751 cm3/g, A1%280 (1 cm) = 6.73 and a specific activity of 183 units/mg towards uridine. The enzyme shows some activity towards deoxyuridine and thymidine. The activity is not impaired through substitution by bromo, fluoro or methyl groups in the 5-position of the uracil base, but no enzymatic activity is observed when cytosine base is used in the nucleoside substrate. |
| Links | |
| Keywords |
Amino Acids/analysis; Drug Stability; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Kinetics; Molecular Weight; Pentosyltransferases/isolation & purification; Protein Conformation; Thymidine Phosphorylase/isolation & purification; Uridine Phosphorylase/isolation & purification; Uridine Phosphorylase/metabolism |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.