Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-165 |
Sentence |
denotes |
A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization. |
TextSentencer_T2 |
166-301 |
Sentence |
denotes |
A congenitally abnormal fibrinogen (Vlissingen) was isolated from the blood of a young woman suffering from massive pulmonary embolism. |
TextSentencer_T3 |
302-390 |
Sentence |
denotes |
Fibrinogen Vlissingen showed an abnormal clotting time with both thrombin and Reptilase. |
TextSentencer_T4 |
391-544 |
Sentence |
denotes |
The release of the fibrino-peptides A and B by thrombin was normal, but fibrin polymerization was impaired both in the presence and absence of Ca2+ ions. |
TextSentencer_T5 |
545-780 |
Sentence |
denotes |
On sodium dodecyl sulfate-polyacrylamide gel electrophoresis performed according to Laemmli the gamma-chain of fibrinogen Vlissingen showed two bands, one normal and one having an apparently lower molecular mass of about 1,500 daltons. |
TextSentencer_T6 |
781-980 |
Sentence |
denotes |
The previously described protective effect of Ca2+ ions on plasmin degradation of the carboxyl terminus of the gamma-chain of normal fibrinogen was only partially detectable in fibrinogen Vlissingen. |
TextSentencer_T7 |
981-1032 |
Sentence |
denotes |
In addition the binding of Ca2+ ions was decreased. |
TextSentencer_T8 |
1033-1156 |
Sentence |
denotes |
Fibrinogen Vlissingen bound 2.4 Ca2+ ions per fibrinogen molecule at pH 7.4, whereas normal fibrinogen bound 3.1 Ca2+ ions. |
TextSentencer_T9 |
1157-1374 |
Sentence |
denotes |
At pH 5.8 fibrinogen Vlissingen bound 1.1 Ca2+ ions, whereas normal fibrinogen bound 2.0 Ca2+ ions per molecule fibrinogen in the D-domains, again indicating a structural change in the carboxyl terminus of fibrinogen. |
TextSentencer_T10 |
1375-1490 |
Sentence |
denotes |
The structural defect was determined by sequence analysis of DNA amplified by use of the polymerase chain reaction. |
TextSentencer_T11 |
1491-1615 |
Sentence |
denotes |
Exons VIII, IX, and X of the gamma-chain gene were amplified and the DNA sequence of the amplified fragments was determined. |
TextSentencer_T12 |
1616-1758 |
Sentence |
denotes |
A 6-base deletion was found in 50% of the fragments corresponding to exon VIII, indicating that the patient was heterozygous for the mutation. |
TextSentencer_T13 |
1759-1852 |
Sentence |
denotes |
This deletion codes for amino acids Asn-319 and Asp-320 in the normal fibrinogen gamma-chain. |
TextSentencer_T14 |
1853-2158 |
Sentence |
denotes |
The data indicate that Asn-319 and Asp-320 are crucial for maintaining the integrity of the carboxyl-terminal polymerization sites, the protective effect of Ca2+ ions on plasmin degradation of the carboxyl terminus of the gamma-chain, and the calcium binding domain at the carboxyl terminus of fibrinogen. |
T1 |
0-165 |
Sentence |
denotes |
A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the gamma-chain gene, causing defective calcium binding and impaired fibrin polymerization. |
T2 |
166-301 |
Sentence |
denotes |
A congenitally abnormal fibrinogen (Vlissingen) was isolated from the blood of a young woman suffering from massive pulmonary embolism. |
T3 |
302-390 |
Sentence |
denotes |
Fibrinogen Vlissingen showed an abnormal clotting time with both thrombin and Reptilase. |
T4 |
391-544 |
Sentence |
denotes |
The release of the fibrino-peptides A and B by thrombin was normal, but fibrin polymerization was impaired both in the presence and absence of Ca2+ ions. |
T5 |
545-780 |
Sentence |
denotes |
On sodium dodecyl sulfate-polyacrylamide gel electrophoresis performed according to Laemmli the gamma-chain of fibrinogen Vlissingen showed two bands, one normal and one having an apparently lower molecular mass of about 1,500 daltons. |
T6 |
781-980 |
Sentence |
denotes |
The previously described protective effect of Ca2+ ions on plasmin degradation of the carboxyl terminus of the gamma-chain of normal fibrinogen was only partially detectable in fibrinogen Vlissingen. |
T7 |
981-1032 |
Sentence |
denotes |
In addition the binding of Ca2+ ions was decreased. |
T8 |
1033-1156 |
Sentence |
denotes |
Fibrinogen Vlissingen bound 2.4 Ca2+ ions per fibrinogen molecule at pH 7.4, whereas normal fibrinogen bound 3.1 Ca2+ ions. |
T9 |
1157-1374 |
Sentence |
denotes |
At pH 5.8 fibrinogen Vlissingen bound 1.1 Ca2+ ions, whereas normal fibrinogen bound 2.0 Ca2+ ions per molecule fibrinogen in the D-domains, again indicating a structural change in the carboxyl terminus of fibrinogen. |
T10 |
1375-1490 |
Sentence |
denotes |
The structural defect was determined by sequence analysis of DNA amplified by use of the polymerase chain reaction. |
T11 |
1491-1615 |
Sentence |
denotes |
Exons VIII, IX, and X of the gamma-chain gene were amplified and the DNA sequence of the amplified fragments was determined. |
T12 |
1616-1758 |
Sentence |
denotes |
A 6-base deletion was found in 50% of the fragments corresponding to exon VIII, indicating that the patient was heterozygous for the mutation. |
T13 |
1759-1852 |
Sentence |
denotes |
This deletion codes for amino acids Asn-319 and Asp-320 in the normal fibrinogen gamma-chain. |
T14 |
1853-2158 |
Sentence |
denotes |
The data indicate that Asn-319 and Asp-320 are crucial for maintaining the integrity of the carboxyl-terminal polymerization sites, the protective effect of Ca2+ ions on plasmin degradation of the carboxyl terminus of the gamma-chain, and the calcium binding domain at the carboxyl terminus of fibrinogen. |