| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-196 |
Sentence |
denotes |
Characterization of glutamate dehydrogenase isoproteins purified from the cerebellum of normal subjects and patients with degenerative neurological disorders, and from human neoplastic cell lines. |
| TextSentencer_T2 |
197-386 |
Sentence |
denotes |
Glutamate dehydrogenase (GDH) was purified to homogeneity from cerebellar tissue of three normal subjects and seven patients with four distinct types of degenerative neurological disorders. |
| TextSentencer_T3 |
387-531 |
Sentence |
denotes |
Nonequilibrium pH gradient gel electrophoresis showed that the purified enzyme consists of four major isoproteins designated GDH 1, 2, 3, and 4. |
| TextSentencer_T4 |
532-719 |
Sentence |
denotes |
With one exception, the relative abundance and isoelectric points of the GDH isoproteins decrease and the molecular weights increase progressively going from isoprotein 1 to isoprotein 4. |
| TextSentencer_T5 |
720-864 |
Sentence |
denotes |
The enzyme isolated from the brain of one patient with a variant form of multiple system atrophy displayed marked reduction of GDH isoprotein 1. |
| TextSentencer_T6 |
865-1053 |
Sentence |
denotes |
The Km values of the patients' GDH for alpha-ketoglutarate, glutamate, NADH, and NADPH were significantly increased as compared to GDH obtained from normal and neurologic control subjects. |
| TextSentencer_T7 |
1054-1134 |
Sentence |
denotes |
In addition, glutamate levels were reduced markedly in the patient's cerebellum. |
| TextSentencer_T8 |
1135-1278 |
Sentence |
denotes |
Pulse-chase studies have shown that both the human hepatoma HepG2 and the human glioma U373 cell lines synthesize exclusively GDH isoprotein 2. |
| TextSentencer_T9 |
1279-1411 |
Sentence |
denotes |
The different GDH isoproteins do not have a precursor-product relationship and may represent products of different GDH mRNA species. |
| T1 |
0-196 |
Sentence |
denotes |
Characterization of glutamate dehydrogenase isoproteins purified from the cerebellum of normal subjects and patients with degenerative neurological disorders, and from human neoplastic cell lines. |
| T2 |
197-386 |
Sentence |
denotes |
Glutamate dehydrogenase (GDH) was purified to homogeneity from cerebellar tissue of three normal subjects and seven patients with four distinct types of degenerative neurological disorders. |
| T3 |
387-531 |
Sentence |
denotes |
Nonequilibrium pH gradient gel electrophoresis showed that the purified enzyme consists of four major isoproteins designated GDH 1, 2, 3, and 4. |
| T4 |
532-719 |
Sentence |
denotes |
With one exception, the relative abundance and isoelectric points of the GDH isoproteins decrease and the molecular weights increase progressively going from isoprotein 1 to isoprotein 4. |
| T5 |
720-864 |
Sentence |
denotes |
The enzyme isolated from the brain of one patient with a variant form of multiple system atrophy displayed marked reduction of GDH isoprotein 1. |
| T6 |
865-1053 |
Sentence |
denotes |
The Km values of the patients' GDH for alpha-ketoglutarate, glutamate, NADH, and NADPH were significantly increased as compared to GDH obtained from normal and neurologic control subjects. |
| T7 |
1054-1134 |
Sentence |
denotes |
In addition, glutamate levels were reduced markedly in the patient's cerebellum. |
| T8 |
1135-1278 |
Sentence |
denotes |
Pulse-chase studies have shown that both the human hepatoma HepG2 and the human glioma U373 cell lines synthesize exclusively GDH isoprotein 2. |
| T9 |
1279-1411 |
Sentence |
denotes |
The different GDH isoproteins do not have a precursor-product relationship and may represent products of different GDH mRNA species. |
