Transformation of 17ß-estradiol to estrone by unknown wild-type enzyme in commercial arylsulfatase from Helix pomatia.
J Chromatogr B Analyt Technol Biomed Life Sci
; 1246: 124293, 2024 Oct 01.
Article
in En
| MEDLINE
| ID: mdl-39236428
ABSTRACT
This work for the first time reported the complete transformation of 17ß-estradiol (E2) to estrone (E1) by unknown wild-type enzyme present in the widely used commercial arylsulfatase derived from Helix pomatia. It was found that acetate could effectively inhibit the unknown enzyme with a half inhibitory concentration (IC50) of 140.9 µM, while phosphate and citrate showed no inhibition. Since the buffer solutions with phosphate and citrate have been used in the enzymatic hydrolysis of natural estrogen conjugates for decades, the transformation of E2 to E1 likely occurred during such procedure, inevitably leading to overestimated E1, but underestimated E2. It was further suggested that acetate should be used to prevent this undesirable transformation during the enzymatic hydrolysis of natural estrogen conjugates.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arylsulfatases
/
Estradiol
/
Estrone
/
Helix, Snails
Limits:
Animals
Language:
En
Journal:
J Chromatogr B Analyt Technol Biomed Life Sci
/
J. chromatogr. B
/
Journal of chromatography. B (Print)
Journal subject:
ENGENHARIA BIOMEDICA
Year:
2024
Document type:
Article
Affiliation country:
China
Country of publication:
Países Bajos