Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-48 |
Sentence |
denotes |
Primary structure of human carbonic anhydrase C. |
T2 |
49-133 |
Sentence |
denotes |
The primary structure of human erythrocyte carbonic anhydrase C has been determined. |
T3 |
134-224 |
Sentence |
denotes |
The single polypeptide chain contains 259 amino acid residues devoid of disulfide bridges. |
T4 |
225-358 |
Sentence |
denotes |
The experimental approach has involved restriction of the action of trypsin to arginyl bonds by amidination of the lysyl side chains. |
T5 |
359-449 |
Sentence |
denotes |
The six tryptic fragments obtained have been separated and sequenced by manual techniques. |
T6 |
450-600 |
Sentence |
denotes |
During the sequence work on human carbonic anhydrase C, 3 very easily deamidated asparagine residues were noted, all occurring in -Asn-Gly- sequences. |
T7 |
601-737 |
Sentence |
denotes |
The deamidation which takes place even under normal conditions of peptide preparation seems to be associated with a beta-aspartyl shift. |
T8 |
738-847 |
Sentence |
denotes |
A few minor differences existing between our structure and the results from another laboratory are discussed. |
T9 |
848-1022 |
Sentence |
denotes |
A brief comparison is made with the primary structures of other carbonic anhydrases with regard to the function of some amino acid residues in the active site of the enzymes. |
T1 |
0-48 |
Sentence |
denotes |
Primary structure of human carbonic anhydrase C. |
T2 |
49-133 |
Sentence |
denotes |
The primary structure of human erythrocyte carbonic anhydrase C has been determined. |
T3 |
134-224 |
Sentence |
denotes |
The single polypeptide chain contains 259 amino acid residues devoid of disulfide bridges. |
T4 |
225-358 |
Sentence |
denotes |
The experimental approach has involved restriction of the action of trypsin to arginyl bonds by amidination of the lysyl side chains. |
T5 |
359-449 |
Sentence |
denotes |
The six tryptic fragments obtained have been separated and sequenced by manual techniques. |
T6 |
450-600 |
Sentence |
denotes |
During the sequence work on human carbonic anhydrase C, 3 very easily deamidated asparagine residues were noted, all occurring in -Asn-Gly- sequences. |
T7 |
601-737 |
Sentence |
denotes |
The deamidation which takes place even under normal conditions of peptide preparation seems to be associated with a beta-aspartyl shift. |
T8 |
738-847 |
Sentence |
denotes |
A few minor differences existing between our structure and the results from another laboratory are discussed. |
T9 |
848-1022 |
Sentence |
denotes |
A brief comparison is made with the primary structures of other carbonic anhydrases with regard to the function of some amino acid residues in the active site of the enzymes. |