Chen L J, Kane B, Bujanover Y, Thaler M M
Biochim Biophys Acta. 1982 Nov 12;713(2):358-64. doi: 10.1016/0005-2760(82)90254-5.
Hepatic bile salt sulfotransferase activity was extremely limited in fetus, gradually increasing after birth. At puberty, enzyme activity declined in males but not in females, suggesting the influence of gonadal hormones associated with sexual maturation. Extremely high enzyme activity was found in pregnant rats at term. The neonatal bile salt sulfotransferase activity could be stimulated by bile acid feeding during pregnancy or maternal bile duct ligation. In contrast, a decrease in enzyme activity was detected in the treated pregnant females. Phenobarbital treatment during pregnancy also produced a 5-fold increase in neonatal enzyme activity. These results suggested that bile salt sulfation was regulated by chemical factors before maturity, and by gonadal hormones thereafter. Two fractions with bile salt sulfotransferase activity were separated from female liver by zone electrophoresis and DEAE-Sephadex A-50 chromatography, while a single active fraction was detected in male liver which corresponded to one of the active female fractions. The two active fractions in the female exhibited the same molecular weight (130 000), and different isoelectric points (6.8 and 5.3). The male fraction had a molecular weight of 130 000 and a pI of 5.3.
胎儿肝脏中的胆盐硫酸转移酶活性极低，出生后逐渐升高。在青春期，该酶活性在男性中下降而在女性中未下降，这表明与性成熟相关的性腺激素的影响。足月妊娠大鼠中发现酶活性极高。孕期胆汁酸喂养或母体胆管结扎可刺激新生鼠胆盐硫酸转移酶活性。相反，在接受治疗的妊娠雌性大鼠中检测到酶活性降低。孕期苯巴比妥治疗也使新生鼠酶活性增加了5倍。这些结果表明，成熟前胆盐硫酸化受化学因素调节，之后受性腺激素调节。通过区带电泳和DEAE-葡聚糖A-50柱层析从雌性肝脏中分离出两个具有胆盐硫酸转移酶活性的组分，而在雄性肝脏中检测到一个单一的活性组分，它与雌性的一个活性组分相对应。雌性中的两个活性组分具有相同的分子量（130 000）和不同的等电点（6.8和5.3）。雄性组分的分子量为130 000，pI为5.3。
