Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-109 |
Sentence |
denotes |
Repair of O6-methylguanine and O4-methylthymine by the human and rat O6-methylguanine-DNA methyltransferases. |
T2 |
110-418 |
Sentence |
denotes |
In order to compare the ability of the human and rat O6-methylguanine-DNA methyltransferases (transferases) to repair in vitro O6-methylguanine (O6-MeGua) and O4-methylthymine (O4-MeThy) residues, which are two mutagenic DNA adducts formed by alkylating agents, we have purified both proteins to homogeneity. |
T3 |
419-582 |
Sentence |
denotes |
Gel electrophoresis of the proteins shows that the O4-MeThy repair is due to the transfer of the methyl group from the alkylated base to the transferase molecules. |
T4 |
583-788 |
Sentence |
denotes |
However, both proteins repair with different efficiencies the O6-MeGua and O4-MeThy residues present in alkylated DNA, poly[d(G.C)], poly(dG.dC), or in alkylated poly[d(A.T)] and poly(dA.dT), respectively. |
T5 |
789-879 |
Sentence |
denotes |
Reaction of both proteins with either methylated residues follows a second-order kinetics. |
T6 |
880-1063 |
Sentence |
denotes |
The rate constants are 1 x 10(9) M-1 min-1 for both proteins acting on O6-MeGua and 4.8 x 10(6) or 1.8 x 10(5) M-1 min-1 for the rat or human protein acting on O4-MeThy, respectively. |
T7 |
1064-1190 |
Sentence |
denotes |
The activity of the mammalian transferases on O4-MeThy present in a poly(dA.dT) substrate is inhibited by double-stranded DNA. |
T1 |
0-109 |
Sentence |
denotes |
Repair of O6-methylguanine and O4-methylthymine by the human and rat O6-methylguanine-DNA methyltransferases. |
T2 |
110-418 |
Sentence |
denotes |
In order to compare the ability of the human and rat O6-methylguanine-DNA methyltransferases (transferases) to repair in vitro O6-methylguanine (O6-MeGua) and O4-methylthymine (O4-MeThy) residues, which are two mutagenic DNA adducts formed by alkylating agents, we have purified both proteins to homogeneity. |
T3 |
419-582 |
Sentence |
denotes |
Gel electrophoresis of the proteins shows that the O4-MeThy repair is due to the transfer of the methyl group from the alkylated base to the transferase molecules. |
T4 |
583-788 |
Sentence |
denotes |
However, both proteins repair with different efficiencies the O6-MeGua and O4-MeThy residues present in alkylated DNA, poly[d(G.C)], poly(dG.dC), or in alkylated poly[d(A.T)] and poly(dA.dT), respectively. |
T5 |
789-879 |
Sentence |
denotes |
Reaction of both proteins with either methylated residues follows a second-order kinetics. |
T6 |
880-1063 |
Sentence |
denotes |
The rate constants are 1 x 10(9) M-1 min-1 for both proteins acting on O6-MeGua and 4.8 x 10(6) or 1.8 x 10(5) M-1 min-1 for the rat or human protein acting on O4-MeThy, respectively. |
T7 |
1064-1190 |
Sentence |
denotes |
The activity of the mammalian transferases on O4-MeThy present in a poly(dA.dT) substrate is inhibited by double-stranded DNA. |