| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-125 |
Sentence |
denotes |
Partial purification of a mannosyltransferase involved in the O-mannosylation of glycoproteins from Saccharomyces cerevisiae. |
| T1 |
0-125 |
Sentence |
denotes |
Partial purification of a mannosyltransferase involved in the O-mannosylation of glycoproteins from Saccharomyces cerevisiae. |
| T1 |
0-125 |
Sentence |
denotes |
Partial purification of a mannosyltransferase involved in the O-mannosylation of glycoproteins from Saccharomyces cerevisiae. |
| TextSentencer_T2 |
126-446 |
Sentence |
denotes |
The mannosyltransferase that catalyses the transfer of mannose from dolichyl-phosphate-mannose (Dol-P-Man) to the hydroxyl group of serine/threonine residues in the acceptor peptide (Tyr-Asn-Pro-Thr-Ser-Val) was partially purified approximately 150-fold from the microsomal membrane fraction of Saccharomyces cerevisiae. |
| T2 |
126-446 |
Sentence |
denotes |
The mannosyltransferase that catalyses the transfer of mannose from dolichyl-phosphate-mannose (Dol-P-Man) to the hydroxyl group of serine/threonine residues in the acceptor peptide (Tyr-Asn-Pro-Thr-Ser-Val) was partially purified approximately 150-fold from the microsomal membrane fraction of Saccharomyces cerevisiae. |
| T2 |
126-446 |
Sentence |
denotes |
The mannosyltransferase that catalyses the transfer of mannose from dolichyl-phosphate-mannose (Dol-P-Man) to the hydroxyl group of serine/threonine residues in the acceptor peptide (Tyr-Asn-Pro-Thr-Ser-Val) was partially purified approximately 150-fold from the microsomal membrane fraction of Saccharomyces cerevisiae. |
| TextSentencer_T3 |
447-670 |
Sentence |
denotes |
The membrane-bound enzyme was solubilized with 0.5% Triton X-100 at a protein:detergent ratio of 2:1, and was then purified by ion-exchange chromatography on DEAE-cellulose, followed by hydroxyapatite column chromatography. |
| T3 |
447-670 |
Sentence |
denotes |
The membrane-bound enzyme was solubilized with 0.5% Triton X-100 at a protein:detergent ratio of 2:1, and was then purified by ion-exchange chromatography on DEAE-cellulose, followed by hydroxyapatite column chromatography. |
| T3 |
447-670 |
Sentence |
denotes |
The membrane-bound enzyme was solubilized with 0.5% Triton X-100 at a protein:detergent ratio of 2:1, and was then purified by ion-exchange chromatography on DEAE-cellulose, followed by hydroxyapatite column chromatography. |
| TextSentencer_T4 |
671-793 |
Sentence |
denotes |
The partially purified enzyme had a pH optimum of 7.2 and required Mg2+ at an optimum concentration of 10 mM for activity. |
| T4 |
671-793 |
Sentence |
denotes |
The partially purified enzyme had a pH optimum of 7.2 and required Mg2+ at an optimum concentration of 10 mM for activity. |
| T4 |
671-793 |
Sentence |
denotes |
The partially purified enzyme had a pH optimum of 7.2 and required Mg2+ at an optimum concentration of 10 mM for activity. |
| TextSentencer_T5 |
794-907 |
Sentence |
denotes |
The apparent mol. wt of the enzyme, as estimated by gel filtration on Sephacryl S-300, was approximately 125 kDa. |
| T5 |
794-907 |
Sentence |
denotes |
The apparent mol. wt of the enzyme, as estimated by gel filtration on Sephacryl S-300, was approximately 125 kDa. |
| T5 |
794-907 |
Sentence |
denotes |
The apparent mol. wt of the enzyme, as estimated by gel filtration on Sephacryl S-300, was approximately 125 kDa. |
| TextSentencer_T6 |
908-1082 |
Sentence |
denotes |
The activity of the partially purified enzyme was greatly stimulated by phosphatidylcholine (PC), while other naturally occurring phosphoglycerides had no significant effect. |
| T6 |
908-1082 |
Sentence |
denotes |
The activity of the partially purified enzyme was greatly stimulated by phosphatidylcholine (PC), while other naturally occurring phosphoglycerides had no significant effect. |
| T6 |
908-1082 |
Sentence |
denotes |
The activity of the partially purified enzyme was greatly stimulated by phosphatidylcholine (PC), while other naturally occurring phosphoglycerides had no significant effect. |
| TextSentencer_T7 |
1083-1331 |
Sentence |
denotes |
The extent of activation of mannosyltransferase activity was greatly affected by the number of carbons and the degree of saturation/unsaturation of the fatty acid substituents, as well as by their position on the glycerol moiety of the PC molecule. |
| T7 |
1083-1331 |
Sentence |
denotes |
The extent of activation of mannosyltransferase activity was greatly affected by the number of carbons and the degree of saturation/unsaturation of the fatty acid substituents, as well as by their position on the glycerol moiety of the PC molecule. |
| T7 |
1083-1331 |
Sentence |
denotes |
The extent of activation of mannosyltransferase activity was greatly affected by the number of carbons and the degree of saturation/unsaturation of the fatty acid substituents, as well as by their position on the glycerol moiety of the PC molecule. |
| TextSentencer_T8 |
1332-1515 |
Sentence |
denotes |
Maximum stimulation of the mannosyltransferase activity was induced by a PC derivative in which both sn-1 and sn-2 positions on the glycerol moiety were occupied by C12:0 fatty acids. |
| T8 |
1332-1515 |
Sentence |
denotes |
Maximum stimulation of the mannosyltransferase activity was induced by a PC derivative in which both sn-1 and sn-2 positions on the glycerol moiety were occupied by C12:0 fatty acids. |
| T8 |
1332-1515 |
Sentence |
denotes |
Maximum stimulation of the mannosyltransferase activity was induced by a PC derivative in which both sn-1 and sn-2 positions on the glycerol moiety were occupied by C12:0 fatty acids. |
| TextSentencer_T9 |
1516-1729 |
Sentence |
denotes |
In general, mannosyltransferase was found to exhibit greater specificity for the L-alpha-PC derivatives in which the sn-2 position of the glycerol contained a saturated fatty acid.(ABSTRACT TRUNCATED AT 250 WORDS) |
| T9 |
1516-1729 |
Sentence |
denotes |
In general, mannosyltransferase was found to exhibit greater specificity for the L-alpha-PC derivatives in which the sn-2 position of the glycerol contained a saturated fatty acid.(ABSTRACT TRUNCATED AT 250 WORDS) |
| T9 |
1516-1729 |
Sentence |
denotes |
In general, mannosyltransferase was found to exhibit greater specificity for the L-alpha-PC derivatives in which the sn-2 position of the glycerol contained a saturated fatty acid.(ABSTRACT TRUNCATED AT 250 WORDS) |