| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-112 |
Sentence |
denotes |
Purification and properties of a 3 beta-hydroxy-delta 5-C27-steroid oxidoreductase from rabbit liver microsomes. |
| T2 |
113-339 |
Sentence |
denotes |
The enzyme converting 5-cholestene-3 beta, 7 alpha-diol to 7 alpha-hydroxy-4-cholesten-3-one has been solubilized from rabbit liver microsomes by treatment with a mixture of sodium cholate and the nonionic detergent Renex 690. |
| T3 |
340-515 |
Sentence |
denotes |
The enzyme was purified about 200-fold, with a recovery of more than 50%, by chromatography on DEAE-cellulose, hydroxylapetite, 2',5',ADP-Sepharose 4B and 5'-AMP-Sepharose 4B. |
| T4 |
516-672 |
Sentence |
denotes |
The purified enzyme showed only one protein band, with an apparent molecular weight of 46,000, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. |
| T5 |
673-749 |
Sentence |
denotes |
The enzyme was eluted as a single peak on gel filtration on Ultrogel AcA 34. |
| T6 |
750-875 |
Sentence |
denotes |
The elution volume corresponded to that observed for globular proteins with molecular weights in the 45,000 to 50,000 region. |
| T7 |
876-1088 |
Sentence |
denotes |
The substrate specificity of the microsomal fraction and of the purified oxidoreductase in oxidation and reduction of various 3-oxygenated C19-, C21-, and C27-steroids was studied in the presence of NAD and NADH. |
| T8 |
1089-1279 |
Sentence |
denotes |
Whereas the microsomal fraction had a broad substrate specificity, NAD-supported oxidation with the purified oxidoreductase only occurred with 5-cholestene-3 beta, 7 alpha-diol as substrate. |
| T9 |
1280-1323 |
Sentence |
denotes |
NADP could not replace NAD in the reaction. |
| T10 |
1324-1454 |
Sentence |
denotes |
NADH-supported reduction with the purified oxidoreductase only occurred with 7 alpha-hydroxy-5 alpha-cholestan-3-one as substrate. |
| T11 |
1455-1631 |
Sentence |
denotes |
The results suggest that conversion of 5-cholestene-3 beta, 7 alpha-diol to 7 alpha-hydroxy-4-cholesten-3-one is catalyzed by a single enzyme specific for certain C27-steroids. |
| T1 |
0-112 |
Sentence |
denotes |
Purification and properties of a 3 beta-hydroxy-delta 5-C27-steroid oxidoreductase from rabbit liver microsomes. |
| T2 |
113-339 |
Sentence |
denotes |
The enzyme converting 5-cholestene-3 beta, 7 alpha-diol to 7 alpha-hydroxy-4-cholesten-3-one has been solubilized from rabbit liver microsomes by treatment with a mixture of sodium cholate and the nonionic detergent Renex 690. |
| T3 |
340-515 |
Sentence |
denotes |
The enzyme was purified about 200-fold, with a recovery of more than 50%, by chromatography on DEAE-cellulose, hydroxylapetite, 2',5',ADP-Sepharose 4B and 5'-AMP-Sepharose 4B. |
| T4 |
516-672 |
Sentence |
denotes |
The purified enzyme showed only one protein band, with an apparent molecular weight of 46,000, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. |
| T5 |
673-749 |
Sentence |
denotes |
The enzyme was eluted as a single peak on gel filtration on Ultrogel AcA 34. |
| T6 |
750-875 |
Sentence |
denotes |
The elution volume corresponded to that observed for globular proteins with molecular weights in the 45,000 to 50,000 region. |
| T7 |
876-1088 |
Sentence |
denotes |
The substrate specificity of the microsomal fraction and of the purified oxidoreductase in oxidation and reduction of various 3-oxygenated C19-, C21-, and C27-steroids was studied in the presence of NAD and NADH. |
| T8 |
1089-1279 |
Sentence |
denotes |
Whereas the microsomal fraction had a broad substrate specificity, NAD-supported oxidation with the purified oxidoreductase only occurred with 5-cholestene-3 beta, 7 alpha-diol as substrate. |
| T9 |
1280-1323 |
Sentence |
denotes |
NADP could not replace NAD in the reaction. |
| T10 |
1324-1454 |
Sentence |
denotes |
NADH-supported reduction with the purified oxidoreductase only occurred with 7 alpha-hydroxy-5 alpha-cholestan-3-one as substrate. |
| T11 |
1455-1631 |
Sentence |
denotes |
The results suggest that conversion of 5-cholestene-3 beta, 7 alpha-diol to 7 alpha-hydroxy-4-cholesten-3-one is catalyzed by a single enzyme specific for certain C27-steroids. |