PMID:5335916
| Citation |
Wolfenden, R, Sharpless, TK and Allan, R (1967) Substrate binding by adenosine deaminase. Specificity, pH dependence, and competition by mercurials. J. Biol. Chem. 242:977-83 |
|---|---|
| Abstract |
No abstract in PubMed |
| Links | |
| Keywords |
Adenine Nucleotides; Aminohydrolases; Animals; Benzoates; Cattle; Chemical Phenomena; Chemistry; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Intestinal Mucosa/enzymology; Kinetics; Mercury; Nucleosides |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
After purification of Ada, there was found to be no complicating metal or cofactor requirements, a broad pH activity range, and also a broad substrate specificity. The enzyme functioned within the pH ranges of 2.7 to 9.5 in .1M glycine buffers, and was insensitive to the concentration of the buffer. The Mercury atom proved to be a competitive inhibitor in mammalian Ada.
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<protect><annotationlinks/></protect>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
