Unknown

Dataset Information

0

Purification and characterization of human liver dehydroepiandrosterone sulphotransferase.


ABSTRACT: A form of sulphotransferase capable of sulphating dehydroepiandrosterone and other steroids was purified from cytosol prepared from human liver. Dehydroepiandrosterone sulphotransferase was purified 621-fold when compared with the activity in cytosol using DEAE-Sepharose CL-6B and adenosine 3',5'-bisphosphate-agarose affinity chromatography. During affinity chromatography, dehydroepiandrosterone sulphation activity could be resolved from p-nitrophenol sulphation activity catalysed by phenol sulphotransferase by using a gradient of adenosine 3'-phosphate 5'-phosphosulphate. The purified enzyme was most active towards dehydroepiandrosterone but was capable of conjugating a number of other steroids, including pregnenolone, androsterone and beta-oestradiol. No activity towards p-nitrophenol or dopamine, substrates for the phenol sulphotransferase, was observed with the pure enzyme. A single band with a subunit molecular mass of 35 kDa was observed by Coomassie Blue staining following SDS/polyacrylamide-gel electrophoresis of the purified enzyme. A molecular mass of 68-70 kDa was calculated for the active form of the enzyme by chromatography on Sephacryl S-200, suggesting that the active form of the enzyme is a dimer.

SUBMITTER: Falany CN 

PROVIDER: S-EPMC1138726 | biostudies-other | 1989 Jun

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1132155 | biostudies-other
| S-EPMC1131791 | biostudies-other
| S-EPMC1132234 | biostudies-other
| S-EPMC5892403 | biostudies-literature
| S-EPMC1223711 | biostudies-other
| S-EPMC1149750 | biostudies-other
| S-EPMC1151634 | biostudies-other
| S-EPMC1163763 | biostudies-other
| S-EPMC3604154 | biostudies-literature
| S-EPMC1144532 | biostudies-other