| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-133 |
Sentence |
denotes |
Glycoprotein biosynthesis in yeast: purification and characterization of the endoplasmic reticulum Man9 processing alpha-mannosidase. |
| T1 |
0-133 |
Sentence |
denotes |
Glycoprotein biosynthesis in yeast: purification and characterization of the endoplasmic reticulum Man9 processing alpha-mannosidase. |
| T1 |
0-133 |
Sentence |
denotes |
Glycoprotein biosynthesis in yeast: purification and characterization of the endoplasmic reticulum Man9 processing alpha-mannosidase. |
| TextSentencer_T2 |
134-419 |
Sentence |
denotes |
Saccharomyces cerevisiae Man9-alpha-mannosidase, responsible for trimming Man9GlcNAc2 in the endoplasmic reticulum to Man8GlcNAc2, the substrate for oligosaccharide elongation, has been purified to homogeneity from stabilized microsomal membranes without employing autolytic digestion. |
| T2 |
134-419 |
Sentence |
denotes |
Saccharomyces cerevisiae Man9-alpha-mannosidase, responsible for trimming Man9GlcNAc2 in the endoplasmic reticulum to Man8GlcNAc2, the substrate for oligosaccharide elongation, has been purified to homogeneity from stabilized microsomal membranes without employing autolytic digestion. |
| T2 |
134-419 |
Sentence |
denotes |
Saccharomyces cerevisiae Man9-alpha-mannosidase, responsible for trimming Man9GlcNAc2 in the endoplasmic reticulum to Man8GlcNAc2, the substrate for oligosaccharide elongation, has been purified to homogeneity from stabilized microsomal membranes without employing autolytic digestion. |
| TextSentencer_T3 |
420-599 |
Sentence |
denotes |
The activity was solubilized by the zwitterionic detergent, 3-[(3-cholamidopropyl)dimethyl ammonio]-1-propanesulphonate (CHAPS), whose presence was necessary for maximal activity. |
| T3 |
420-599 |
Sentence |
denotes |
The activity was solubilized by the zwitterionic detergent, 3-[(3-cholamidopropyl)dimethyl ammonio]-1-propanesulphonate (CHAPS), whose presence was necessary for maximal activity. |
| T3 |
420-599 |
Sentence |
denotes |
The activity was solubilized by the zwitterionic detergent, 3-[(3-cholamidopropyl)dimethyl ammonio]-1-propanesulphonate (CHAPS), whose presence was necessary for maximal activity. |
| TextSentencer_T4 |
600-739 |
Sentence |
denotes |
Purification included Q-Sepharose ion-exchange chromatography, preparative isoelectric focusing and HPLC gel filtration on TSK 3000 matrix. |
| T4 |
600-739 |
Sentence |
denotes |
Purification included Q-Sepharose ion-exchange chromatography, preparative isoelectric focusing and HPLC gel filtration on TSK 3000 matrix. |
| T4 |
600-739 |
Sentence |
denotes |
Purification included Q-Sepharose ion-exchange chromatography, preparative isoelectric focusing and HPLC gel filtration on TSK 3000 matrix. |
| TextSentencer_T5 |
740-857 |
Sentence |
denotes |
Overall purification from post-nuclear supernatants was estimated to be 110,000-fold with a 50% recovery of activity. |
| T5 |
740-857 |
Sentence |
denotes |
Overall purification from post-nuclear supernatants was estimated to be 110,000-fold with a 50% recovery of activity. |
| T5 |
740-857 |
Sentence |
denotes |
Overall purification from post-nuclear supernatants was estimated to be 110,000-fold with a 50% recovery of activity. |
| TextSentencer_T6 |
858-1047 |
Sentence |
denotes |
The purified enzyme hydrolysed Man9GlcNAc1,2 from thyroglobulin or oligosaccharide-lipid, but not invertase Man9GlcNAc, Man1 alpha 2Man1 alpha OCH3 or p-nitrophenyl-alpha-D-mannopyranoside. |
| T6 |
858-1047 |
Sentence |
denotes |
The purified enzyme hydrolysed Man9GlcNAc1,2 from thyroglobulin or oligosaccharide-lipid, but not invertase Man9GlcNAc, Man1 alpha 2Man1 alpha OCH3 or p-nitrophenyl-alpha-D-mannopyranoside. |
| T6 |
858-1047 |
Sentence |
denotes |
The purified enzyme hydrolysed Man9GlcNAc1,2 from thyroglobulin or oligosaccharide-lipid, but not invertase Man9GlcNAc, Man1 alpha 2Man1 alpha OCH3 or p-nitrophenyl-alpha-D-mannopyranoside. |
| TextSentencer_T7 |
1048-1215 |
Sentence |
denotes |
Conversion of thyroglobulin Man9GlcNAc to Man8GlcNAc was linear with time and enzyme concentration, with an apparent Km of 0.2 mM and a specific activity of 220 IU/mg. |
| T7 |
1048-1215 |
Sentence |
denotes |
Conversion of thyroglobulin Man9GlcNAc to Man8GlcNAc was linear with time and enzyme concentration, with an apparent Km of 0.2 mM and a specific activity of 220 IU/mg. |
| T7 |
1048-1215 |
Sentence |
denotes |
Conversion of thyroglobulin Man9GlcNAc to Man8GlcNAc was linear with time and enzyme concentration, with an apparent Km of 0.2 mM and a specific activity of 220 IU/mg. |
| TextSentencer_T8 |
1216-1378 |
Sentence |
denotes |
Glc3Man9GlcNAc2 from oligosaccharide-lipid was as good a substrate as Man9GlcNAc, but the lipid-linked Man7GlcNAc2 isomer was hydrolysed at only 10% of this rate. |
| T8 |
1216-1378 |
Sentence |
denotes |
Glc3Man9GlcNAc2 from oligosaccharide-lipid was as good a substrate as Man9GlcNAc, but the lipid-linked Man7GlcNAc2 isomer was hydrolysed at only 10% of this rate. |
| T8 |
1216-1378 |
Sentence |
denotes |
Glc3Man9GlcNAc2 from oligosaccharide-lipid was as good a substrate as Man9GlcNAc, but the lipid-linked Man7GlcNAc2 isomer was hydrolysed at only 10% of this rate. |
| TextSentencer_T9 |
1379-1627 |
Sentence |
denotes |
Hydrolysis of defined isomers of IgM and bovine thyroglobulin Man6,7,8GlcNAc indicated that, for maximal alpha 1,2-mannosidase activity, only the alpha 1,2-linked terminal mannoses on the alpha 3 branch of the Man9GlcNAc precursor were dispensable. |
| T9 |
1379-1627 |
Sentence |
denotes |
Hydrolysis of defined isomers of IgM and bovine thyroglobulin Man6,7,8GlcNAc indicated that, for maximal alpha 1,2-mannosidase activity, only the alpha 1,2-linked terminal mannoses on the alpha 3 branch of the Man9GlcNAc precursor were dispensable. |
| T9 |
1379-1627 |
Sentence |
denotes |
Hydrolysis of defined isomers of IgM and bovine thyroglobulin Man6,7,8GlcNAc indicated that, for maximal alpha 1,2-mannosidase activity, only the alpha 1,2-linked terminal mannoses on the alpha 3 branch of the Man9GlcNAc precursor were dispensable. |
| TextSentencer_T10 |
1628-1766 |
Sentence |
denotes |
Isomers lacking the terminal alpha 1,2-linked mannose on the alpha 6 branch were hydrolysed at only approximately 10% of the maximal rate. |
| T10 |
1628-1766 |
Sentence |
denotes |
Isomers lacking the terminal alpha 1,2-linked mannose on the alpha 6 branch were hydrolysed at only approximately 10% of the maximal rate. |
| T10 |
1628-1766 |
Sentence |
denotes |
Isomers lacking the terminal alpha 1,2-linked mannose on the alpha 6 branch were hydrolysed at only approximately 10% of the maximal rate. |
| TextSentencer_T11 |
1767-1824 |
Sentence |
denotes |
The enzyme exhibited a pI of 5.3 and a pH optimum at 6.5. |
| T11 |
1767-1824 |
Sentence |
denotes |
The enzyme exhibited a pI of 5.3 and a pH optimum at 6.5. |
| T11 |
1767-1824 |
Sentence |
denotes |
The enzyme exhibited a pI of 5.3 and a pH optimum at 6.5. |
| TextSentencer_T12 |
1825-2082 |
Sentence |
denotes |
Sodium dodecyl sulphate-polyacrylamide gel electrophoresis in the absence of reducing agents gave a single sharp band at 66 kDa, while in the presence of beta-mercaptoethanol equimolar amounts of two peptides, one of 44 kDa and one of 23 kDa, were obtained. |
| T12 |
1825-2082 |
Sentence |
denotes |
Sodium dodecyl sulphate-polyacrylamide gel electrophoresis in the absence of reducing agents gave a single sharp band at 66 kDa, while in the presence of beta-mercaptoethanol equimolar amounts of two peptides, one of 44 kDa and one of 23 kDa, were obtained. |
| T12 |
1825-2082 |
Sentence |
denotes |
Sodium dodecyl sulphate-polyacrylamide gel electrophoresis in the absence of reducing agents gave a single sharp band at 66 kDa, while in the presence of beta-mercaptoethanol equimolar amounts of two peptides, one of 44 kDa and one of 23 kDa, were obtained. |
| TextSentencer_T13 |
2083-2320 |
Sentence |
denotes |
Sizing on Sephacryl SF300, Superose 12 and TSK 3000 provided a holoenzyme mol. wt of 60-68 kDa, indicating that the isolated active form of the Man9-alpha-mannosidase was composed of one each of the sulphydryl-bonded dissimilar peptides. |
| T13 |
2083-2320 |
Sentence |
denotes |
Sizing on Sephacryl SF300, Superose 12 and TSK 3000 provided a holoenzyme mol. wt of 60-68 kDa, indicating that the isolated active form of the Man9-alpha-mannosidase was composed of one each of the sulphydryl-bonded dissimilar peptides. |
| T13 |
2083-2320 |
Sentence |
denotes |
Sizing on Sephacryl SF300, Superose 12 and TSK 3000 provided a holoenzyme mol. wt of 60-68 kDa, indicating that the isolated active form of the Man9-alpha-mannosidase was composed of one each of the sulphydryl-bonded dissimilar peptides. |
| TextSentencer_T14 |
2321-2473 |
Sentence |
denotes |
The enzyme bound to concanavalin A (ConA)-Sepharose and was eluted with alpha-methylmannoside, indicating the presence of high-mannose oligosaccharides. |
| T14 |
2321-2473 |
Sentence |
denotes |
The enzyme bound to concanavalin A (ConA)-Sepharose and was eluted with alpha-methylmannoside, indicating the presence of high-mannose oligosaccharides. |
| T14 |
2321-2473 |
Sentence |
denotes |
The enzyme bound to concanavalin A (ConA)-Sepharose and was eluted with alpha-methylmannoside, indicating the presence of high-mannose oligosaccharides. |
| TextSentencer_T15 |
2474-2561 |
Sentence |
denotes |
The Man9-alpha-mannosidase required low levels of Ca2+, which could be removed by EGTA. |
| T15 |
2474-2561 |
Sentence |
denotes |
The Man9-alpha-mannosidase required low levels of Ca2+, which could be removed by EGTA. |
| T15 |
2474-2561 |
Sentence |
denotes |
The Man9-alpha-mannosidase required low levels of Ca2+, which could be removed by EGTA. |
| TextSentencer_T16 |
2562-2625 |
Sentence |
denotes |
Activity was restored by Ca2+ or Zn2+, but not by Mg2+ or Mn2+. |
| T16 |
2562-2625 |
Sentence |
denotes |
Activity was restored by Ca2+ or Zn2+, but not by Mg2+ or Mn2+. |
| T16 |
2562-2625 |
Sentence |
denotes |
Activity was restored by Ca2+ or Zn2+, but not by Mg2+ or Mn2+. |