Chen L J, Rosenquist G L
Department of Internal Medicine, University of California, Davis.
Biochem Biophys Res Commun. 1990 Aug 16;170(3):1170-6. doi: 10.1016/0006-291x(90)90516-p.
An enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to gastrin (G17) was identified in rat gastric mucosal cells. The enzyme activity was detected in the 105,000xg supernatant fraction. Formation of gastrin sulfate was shown by using 125I-gastrin and non-radioactive PAPS. The product was sensitive to acid hydrolysis, arylsulfatase treatment and removed by gastrin antibody, but not changed by treatments with chondro-4-sulfatase and chondro-6-sulfatase. The product had a molecular weight of 2050 daltons, close to the molecular weight of G17 sulfate, and, therefore, indicating the sulfated product is not APS derived from the degradation of PAPS. The enzyme activity showed a Km value of 5 microM for PAPS and a pH optimum of 6.0. The activity was not detected in the liver preparation.
在大鼠胃黏膜细胞中发现了一种能催化将硫酸根从3'-磷酸腺苷5'-磷酸硫酸酯（PAPS）转移至胃泌素（G17）的酶。该酶活性在105,000xg超速离心上清组分中被检测到。利用125I-胃泌素和非放射性PAPS证实了硫酸化胃泌素的形成。产物对酸水解、芳基硫酸酯酶处理敏感，可被胃泌素抗体去除，但经软骨素-4-硫酸酯酶和软骨素-6-硫酸酯酶处理后不变。产物分子量为2050道尔顿，与硫酸化G17的分子量相近，因此表明硫酸化产物并非源自PAPS降解产生的APS。该酶活性对PAPS的Km值为5 microM，最适pH为6.0。在肝脏制剂中未检测到该活性。
