| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-90 |
Sentence |
denotes |
Identification and purification of a calcium-binding protein in hepatic nuclear membranes. |
| T2 |
91-213 |
Sentence |
denotes |
Recent evidence suggests that nuclei possess Ca2+ transport mechanisms to regulate nucleoplasmic/cytosolic Ca2+ gradients. |
| T3 |
214-321 |
Sentence |
denotes |
We, therefore, investigated the possibility that Ca(2+)-binding proteins may also exist within the nucleus. |
| T4 |
322-689 |
Sentence |
denotes |
Electrophoretic analysis revealed the presence of an acidic 93-kDa protein (p93) in the membranes of isolated nuclei. p93 stained blue with "Stains-All" in SDS-polyacrylamide gels and was the major 45Ca(2+)- and ruthenium red-binding nuclear envelope protein in electroblot overlays. p93 was resistant to extraction by 6 M urea but was solubilized in 2% Triton X-100. |
| T5 |
690-853 |
Sentence |
denotes |
Citric acid was highly effective in removing the outer nuclear membrane (ER) with concomitant reduction (< 10-fold) of mannose-6-phosphatase activity, but not p93. |
| T6 |
854-981 |
Sentence |
denotes |
45Ca(2+)-binding assays of purified p93 revealed the presence of high capacity Ca(2+)-binding sites comparable to calreticulin. |
| T7 |
982-1096 |
Sentence |
denotes |
This evidence strongly suggests that p93 is a major Ca(2+)-binding protein of the inner nuclear envelope membrane. |
| T8 |
1097-1252 |
Sentence |
denotes |
Partial amino acid sequence analysis revealed that p93 was close to 100% homologous with a recently identified ER Ca(2+)-binding protein known as calnexin. |
| T9 |
1253-1299 |
Sentence |
denotes |
It is likely, therefore, that p93 is calnexin. |
| T10 |
1300-1463 |
Sentence |
denotes |
However, mild CHAPS detergent treatment of nuclear envelopes and ER revealed distinctly different solubility properties of each membrane for the extraction of p93. |
| T11 |
1464-1608 |
Sentence |
denotes |
This, together with the citrate data, strongly suggests that p93/calnexin, in isolated nuclear envelopes, is mostly bound to the inner membrane. |
| T12 |
1609-1734 |
Sentence |
denotes |
It is possible that p93 may be involved with the regulation of Ca2+ transients between the nucleoplasm and perinuclear space. |
| T1 |
0-90 |
Sentence |
denotes |
Identification and purification of a calcium-binding protein in hepatic nuclear membranes. |
| T2 |
91-213 |
Sentence |
denotes |
Recent evidence suggests that nuclei possess Ca2+ transport mechanisms to regulate nucleoplasmic/cytosolic Ca2+ gradients. |
| T3 |
214-321 |
Sentence |
denotes |
We, therefore, investigated the possibility that Ca(2+)-binding proteins may also exist within the nucleus. |
| T4 |
322-689 |
Sentence |
denotes |
Electrophoretic analysis revealed the presence of an acidic 93-kDa protein (p93) in the membranes of isolated nuclei. p93 stained blue with "Stains-All" in SDS-polyacrylamide gels and was the major 45Ca(2+)- and ruthenium red-binding nuclear envelope protein in electroblot overlays. p93 was resistant to extraction by 6 M urea but was solubilized in 2% Triton X-100. |
| T5 |
690-853 |
Sentence |
denotes |
Citric acid was highly effective in removing the outer nuclear membrane (ER) with concomitant reduction (< 10-fold) of mannose-6-phosphatase activity, but not p93. |
| T6 |
854-981 |
Sentence |
denotes |
45Ca(2+)-binding assays of purified p93 revealed the presence of high capacity Ca(2+)-binding sites comparable to calreticulin. |
| T7 |
982-1096 |
Sentence |
denotes |
This evidence strongly suggests that p93 is a major Ca(2+)-binding protein of the inner nuclear envelope membrane. |
| T8 |
1097-1252 |
Sentence |
denotes |
Partial amino acid sequence analysis revealed that p93 was close to 100% homologous with a recently identified ER Ca(2+)-binding protein known as calnexin. |
| T9 |
1253-1299 |
Sentence |
denotes |
It is likely, therefore, that p93 is calnexin. |
| T10 |
1300-1463 |
Sentence |
denotes |
However, mild CHAPS detergent treatment of nuclear envelopes and ER revealed distinctly different solubility properties of each membrane for the extraction of p93. |
| T11 |
1464-1608 |
Sentence |
denotes |
This, together with the citrate data, strongly suggests that p93/calnexin, in isolated nuclear envelopes, is mostly bound to the inner membrane. |
| T12 |
1609-1734 |
Sentence |
denotes |
It is possible that p93 may be involved with the regulation of Ca2+ transients between the nucleoplasm and perinuclear space. |