| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-93 |
Sentence |
denotes |
Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein. |
| T2 |
94-272 |
Sentence |
denotes |
Eosinophil granule major basic protein (MBP) is a relatively low molecular weight cationic (pI greater than 10) protein present in the crystalloid core of the eosinophil granule. |
| T3 |
273-455 |
Sentence |
denotes |
Amino acid sequence analysis of this protein was undertaken as part of an analysis of the structural basis of the potent cytotoxic activities of MBP on parasites and mammalian cells. |
| T4 |
456-622 |
Sentence |
denotes |
Many conventional sequencing strategies were unworkable because of the unusual amino acid composition of MBP and its insolubility in solutions buffered at neutral pH. |
| T5 |
623-864 |
Sentence |
denotes |
Less conventional chemical reactions, including cyanogen bromide-induced cleavage at tryptophan and acid-induced cleavage at aspartic acid, were used successfully to obtain peptides which allowed definition of the amino acid sequence of MBP. |
| T6 |
865-1065 |
Sentence |
denotes |
Characterization of MBP by reverse-phase high pressure liquid chromatography and two-dimensional gel analysis showed no microheterogeneity that might be attributed to post-translational modifications. |
| T7 |
1066-1218 |
Sentence |
denotes |
Comparison of the MBP sequence with a protein sequence data base showed that MBP has no significant sequence homology with other characterized proteins. |
| T8 |
1219-1411 |
Sentence |
denotes |
The basicity (pI 10.9) and hydrophobicity predicted from the MBP sequence are likely responsible for the observed affinity of this cytotoxic molecule for cell surfaces and some serum proteins. |
| T1 |
0-93 |
Sentence |
denotes |
Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein. |
| T2 |
94-272 |
Sentence |
denotes |
Eosinophil granule major basic protein (MBP) is a relatively low molecular weight cationic (pI greater than 10) protein present in the crystalloid core of the eosinophil granule. |
| T3 |
273-455 |
Sentence |
denotes |
Amino acid sequence analysis of this protein was undertaken as part of an analysis of the structural basis of the potent cytotoxic activities of MBP on parasites and mammalian cells. |
| T4 |
456-622 |
Sentence |
denotes |
Many conventional sequencing strategies were unworkable because of the unusual amino acid composition of MBP and its insolubility in solutions buffered at neutral pH. |
| T5 |
623-864 |
Sentence |
denotes |
Less conventional chemical reactions, including cyanogen bromide-induced cleavage at tryptophan and acid-induced cleavage at aspartic acid, were used successfully to obtain peptides which allowed definition of the amino acid sequence of MBP. |
| T6 |
865-1065 |
Sentence |
denotes |
Characterization of MBP by reverse-phase high pressure liquid chromatography and two-dimensional gel analysis showed no microheterogeneity that might be attributed to post-translational modifications. |
| T7 |
1066-1218 |
Sentence |
denotes |
Comparison of the MBP sequence with a protein sequence data base showed that MBP has no significant sequence homology with other characterized proteins. |
| T8 |
1219-1411 |
Sentence |
denotes |
The basicity (pI 10.9) and hydrophobicity predicted from the MBP sequence are likely responsible for the observed affinity of this cytotoxic molecule for cell surfaces and some serum proteins. |