PMID:5335916: Difference between revisions
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
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 {{HelpIcon|Help:Literature}}== | == Useful Materials and Methods {{HelpIcon|Help:Literature}}== | ||
Revision as of 17:55, 24 February 2009
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 |
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Significance
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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
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Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
Add |
GO:0004000 |
adenosine deaminase activity |
ISS: Inferred from Sequence or Structural Similarity |
F |
complete | |||
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EcoliWiki Links
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