Abstract
The activity of "cholinesterase" in human blood serum with the sodium salts of a homologous series of n-fatty acid esters of m-hydroxybenzoic acid as the substrates increases in a characteristic manner with increasing acyl carbon chain length up to at least 10 C atoms.
Depending on the substrate and its concentration, the enzymic hydrolysis of these anionic esters is increased up to the order of 20- to 30-fold by certain bivalent metal ions, notably Mg++, Ca++, Sr++, Ba++ and Mn++, but these ions are not essential for activity.
The results provide an improvement of a direct and continuous spectrophotometric method for the assay of serum cholinesterase presented previously.
Footnotes
- Received December 9, 1957.
JPET articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|
Log in using your username and password
Purchase access
You may purchase access to this article. This will require you to create an account if you don't already have one.
In this issue
Jump to section
Related Articles
Cited By...
More in this TOC Section
Similar Articles
Advertisement