Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-112 |
Sentence |
denotes |
Complete primary structure of a newly characterized galactose-specific lectin from the seeds of Dolichos lablab. |
TextSentencer_T2 |
113-288 |
Sentence |
denotes |
A new unique lectin (galactose-specific) purified from the seeds of Dolichos lablab, designated as DLL-II is a heterodimer composed of closely related subunits alpha and beta. |
TextSentencer_T3 |
289-353 |
Sentence |
denotes |
These were separated by SDS-PAGE and isolated by electroelution. |
TextSentencer_T4 |
354-467 |
Sentence |
denotes |
By ESI-MS analysis their molecular masses were found to be 30.746 kDa (alpha) and 28.815 kDa (beta) respectively. |
TextSentencer_T5 |
468-545 |
Sentence |
denotes |
Both subunits were glycosylated and displayed similar amino acid composition. |
TextSentencer_T6 |
546-752 |
Sentence |
denotes |
Using advanced mass spectrometry in combination with de novo sequencing and database searches for the peptides derived by enzymatic and chemical cleavage of these subunits, the primary sequence was deduced. |
TextSentencer_T7 |
753-864 |
Sentence |
denotes |
This revealed DLL-II to be made of two polypeptide chains of 281(alpha) and 263(beta) amino acids respectively. |
TextSentencer_T8 |
865-977 |
Sentence |
denotes |
The beta subunit differed from the alpha subunit by the absence of some amino acids at the carboxy terminal end. |
TextSentencer_T9 |
978-1147 |
Sentence |
denotes |
This structural difference suggests that possibly, the beta subunit is derived from the alpha subunit by posttranslational proteolytic modification at the COOH-terminus. |
TextSentencer_T10 |
1148-1266 |
Sentence |
denotes |
Comparison of the DLL-II sequence to other leguminous seed lectins indicates a high degree of structural conservation. |
T1 |
0-112 |
Sentence |
denotes |
Complete primary structure of a newly characterized galactose-specific lectin from the seeds of Dolichos lablab. |
T2 |
113-288 |
Sentence |
denotes |
A new unique lectin (galactose-specific) purified from the seeds of Dolichos lablab, designated as DLL-II is a heterodimer composed of closely related subunits alpha and beta. |
T3 |
289-353 |
Sentence |
denotes |
These were separated by SDS-PAGE and isolated by electroelution. |
T4 |
354-467 |
Sentence |
denotes |
By ESI-MS analysis their molecular masses were found to be 30.746 kDa (alpha) and 28.815 kDa (beta) respectively. |
T5 |
468-545 |
Sentence |
denotes |
Both subunits were glycosylated and displayed similar amino acid composition. |
T6 |
546-752 |
Sentence |
denotes |
Using advanced mass spectrometry in combination with de novo sequencing and database searches for the peptides derived by enzymatic and chemical cleavage of these subunits, the primary sequence was deduced. |
T7 |
753-864 |
Sentence |
denotes |
This revealed DLL-II to be made of two polypeptide chains of 281(alpha) and 263(beta) amino acids respectively. |
T8 |
865-977 |
Sentence |
denotes |
The beta subunit differed from the alpha subunit by the absence of some amino acids at the carboxy terminal end. |
T9 |
978-1147 |
Sentence |
denotes |
This structural difference suggests that possibly, the beta subunit is derived from the alpha subunit by posttranslational proteolytic modification at the COOH-terminus. |
T10 |
1148-1266 |
Sentence |
denotes |
Comparison of the DLL-II sequence to other leguminous seed lectins indicates a high degree of structural conservation. |