| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-179 |
Sentence |
denotes |
The functional characteristics of a human apolipoprotein E variant (cysteine at residue 142) may explain its association with dominant expression of type III hyperlipoproteinemia. |
| T2 |
180-295 |
Sentence |
denotes |
Type III hyperlipoproteinemia typically is associated with homozygosity for apolipoprotein (apo) E2(Arg158----Cys). |
| T3 |
296-475 |
Sentence |
denotes |
Dominant expression of type III hyperlipoproteinemia associated with apoE phenotype E3/3 is caused by heterozygosity for a human apoE variant, apoE3(Cys112----Arg, Arg142----Cys). |
| T4 |
476-663 |
Sentence |
denotes |
However, this apoE3 variant was not separable from the normal apoE3 in these patients' plasma because the two proteins have identical amino acid composition, charge, and molecular weight. |
| T5 |
664-812 |
Sentence |
denotes |
Therefore, to determine the functional characteristics of this protein, we used recombinant DNA techniques to produce this apoE variant in bacteria. |
| T6 |
813-940 |
Sentence |
denotes |
We also produced a non-naturally occurring variant, apoE(Arg142----Cys), that had only the cysteine substituted at residue 142. |
| T7 |
941-1170 |
Sentence |
denotes |
These two apoE variants were purified from cell lysates of the transfected Escherichia coli by ultracentrifugal flotation in the presence of phospholipid, by gel filtration chromatography, and by heparin-Sepharose chromatography. |
| T8 |
1171-1296 |
Sentence |
denotes |
Both Cys142 apoE variants bound to lipoprotein receptors on human fibroblasts with only about 20% of normal binding activity. |
| T9 |
1297-1437 |
Sentence |
denotes |
Therefore, cysteine at residue 142, not arginine at residue 112, is responsible for the decreased receptor binding activity of the variants. |
| T10 |
1438-1622 |
Sentence |
denotes |
Cysteamine treatment and removal of the carboxyl-terminal domain had little effect on the binding activity, whereas both modulate the receptor binding activity of apoE2(Arg158----Cys). |
| T11 |
1623-1922 |
Sentence |
denotes |
The mutation at residue 142 decreased the binding activity of apoE to both heparin and the monoclonal antibody 1D7 (this antibody inhibits receptor binding of apoE), whereas apoE2(Arg158----Cys), which is associated with recessive expression of type III hyperlipoproteinemia, binds normally to both. |
| T12 |
1923-2120 |
Sentence |
denotes |
The Arg112, Cys142 variant predominantes 3:1 over normal apoE3 in the very low density lipoproteins of plasma from an affected subject, as assessed by differential reactivity with the antibody 1D7. |
| T13 |
2121-2309 |
Sentence |
denotes |
The unique combination of functional properties of the Arg112, Cys142 variant provides a possible explanation for its association with dominant expression of type III hyperlipoproteinemia. |
| T1 |
0-179 |
Sentence |
denotes |
The functional characteristics of a human apolipoprotein E variant (cysteine at residue 142) may explain its association with dominant expression of type III hyperlipoproteinemia. |
| T2 |
180-295 |
Sentence |
denotes |
Type III hyperlipoproteinemia typically is associated with homozygosity for apolipoprotein (apo) E2(Arg158----Cys). |
| T3 |
296-475 |
Sentence |
denotes |
Dominant expression of type III hyperlipoproteinemia associated with apoE phenotype E3/3 is caused by heterozygosity for a human apoE variant, apoE3(Cys112----Arg, Arg142----Cys). |
| T4 |
476-663 |
Sentence |
denotes |
However, this apoE3 variant was not separable from the normal apoE3 in these patients' plasma because the two proteins have identical amino acid composition, charge, and molecular weight. |
| T5 |
664-812 |
Sentence |
denotes |
Therefore, to determine the functional characteristics of this protein, we used recombinant DNA techniques to produce this apoE variant in bacteria. |
| T6 |
813-940 |
Sentence |
denotes |
We also produced a non-naturally occurring variant, apoE(Arg142----Cys), that had only the cysteine substituted at residue 142. |
| T7 |
941-1170 |
Sentence |
denotes |
These two apoE variants were purified from cell lysates of the transfected Escherichia coli by ultracentrifugal flotation in the presence of phospholipid, by gel filtration chromatography, and by heparin-Sepharose chromatography. |
| T8 |
1171-1296 |
Sentence |
denotes |
Both Cys142 apoE variants bound to lipoprotein receptors on human fibroblasts with only about 20% of normal binding activity. |
| T9 |
1297-1437 |
Sentence |
denotes |
Therefore, cysteine at residue 142, not arginine at residue 112, is responsible for the decreased receptor binding activity of the variants. |
| T10 |
1438-1622 |
Sentence |
denotes |
Cysteamine treatment and removal of the carboxyl-terminal domain had little effect on the binding activity, whereas both modulate the receptor binding activity of apoE2(Arg158----Cys). |
| T11 |
1623-1922 |
Sentence |
denotes |
The mutation at residue 142 decreased the binding activity of apoE to both heparin and the monoclonal antibody 1D7 (this antibody inhibits receptor binding of apoE), whereas apoE2(Arg158----Cys), which is associated with recessive expression of type III hyperlipoproteinemia, binds normally to both. |
| T12 |
1923-2120 |
Sentence |
denotes |
The Arg112, Cys142 variant predominantes 3:1 over normal apoE3 in the very low density lipoproteins of plasma from an affected subject, as assessed by differential reactivity with the antibody 1D7. |
| T13 |
2121-2309 |
Sentence |
denotes |
The unique combination of functional properties of the Arg112, Cys142 variant provides a possible explanation for its association with dominant expression of type III hyperlipoproteinemia. |