MOLECULAR-CLONING AND FUNCTIONS OF RAT-LIVER HYDROXYSTEROID SULFOTRANSFERASES CATALYZING COVALENT BINDING OF CARCINOGENIC POLYCYCLIC ARYLMETHANOLS TO DNA
T. Watabe et al., MOLECULAR-CLONING AND FUNCTIONS OF RAT-LIVER HYDROXYSTEROID SULFOTRANSFERASES CATALYZING COVALENT BINDING OF CARCINOGENIC POLYCYCLIC ARYLMETHANOLS TO DNA, Chemico-biological interactions, 92(1-3), 1994, pp. 87-105
Three sulfotransferases (STs) catalysing the metabolic activation of p
otent carcinogenic polycyclic arylmethanols were purified from female
Sprague-Dawley (SD) rat liver cytosol without loss of their enzyme act
ivities in the presence of Tween 20 used for preventing the enzymes fr
om aggregation during purification and identified as hydroxysteroid su
lfotransferases (HSTs). All the purified HSTs, STa, STb, and STc, with
different electric charges had an apparently equal size of subunit (3
0.5 kDa) and cross-reacted with polyclonal antibody raised against STa
. Our study on molecular cloning of cDNA libraries from two female SD
rat livers indicated that both contained cDNA inserts coding for 5 dif
ferent HST subunits, consisting of 284-285 amino acid residues (M tau,
33 084-33 535) and sharing strong amino acid sequence identity (> 83%
). Of the 5 HST subunits, two had an identical amino acid sequence exc
ept for only one amino acid residue, and the other two contained only
6 amino acid substitutions in their sequences.