| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-94 |
Sentence |
denotes |
Characterization and localization of the sporulation glucoamylase of Saccharomyces cerevisiae. |
| T2 |
95-198 |
Sentence |
denotes |
Glucoamylase (SGA) was purified approximately 250-fold from sporulating Saccharomyces cerevisiae cells. |
| T3 |
199-290 |
Sentence |
denotes |
The partially purified enzyme was active against glycogen, starch, maltotriose and maltose. |
| T4 |
291-358 |
Sentence |
denotes |
It exhibited maximum catalytic activity against glycogen at pH 5.5. |
| T5 |
359-622 |
Sentence |
denotes |
The enzyme appears to be glycosylated, because it bound to lentil-lectin Sepharose. SGA was expressed in vegetatively growing cells under the control of the GAL1 promoter, and the cellular location of the enzymatic activity determined by fractionation techniques. |
| T6 |
623-759 |
Sentence |
denotes |
SGA was preferentially recovered in fractions which were enriched for the vacuolar hydrolases, carboxypeptidase Y and alpha-mannosidase. |
