PMID:16751: Difference between revisions

From EcoliWiki
Jump to navigation Jump to search
← Older editNewer edit →
/Volumes/r3/t3/ul/working/touchTables/touch_all_tables.php
imported>Wikientrybot
change PMID template to TableEdit version
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" 


<span style = 'font-size: large'> '''Leer, JC, Hammer-Jespersen, K and Schwartz, M'''  (1977) Uridine phosphorylase from Escherichia coli. Physical and chemical characterization.''Eur. J. Biochem.'' '''75''':217-24</span>
|-
!align=left  |Citation
||
'''No author listed'''  (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]


{|{{Prettytable}} align = 'center' width= '70%'
|-
|-
|{{TableHeadingColor}} |'''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  |Keywords
</noinclude>
||
|-
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
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16751 PubMed]
 
|- 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}}

Revision as of 18:53, 1 September 2013

Citation

No author listed (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

PubMed

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

Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status
edit table

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.

Retrieved from "https://ecoliwiki.org/colipedia/index.php?title=PMID:16751&oldid=1423066"