Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-53 |
Sentence |
denotes |
Inositol polyphosphate 1-phosphatase from calf brain. |
T1 |
0-53 |
Sentence |
denotes |
Inositol polyphosphate 1-phosphatase from calf brain. |
T2 |
54-105 |
Sentence |
denotes |
Purification and inhibition by Li+, Ca2+, and Mn2+. |
T2 |
54-105 |
Sentence |
denotes |
Purification and inhibition by Li+, Ca2+, and Mn2+. |
T3 |
106-408 |
Sentence |
denotes |
We recently identified an enzyme which we have designated inositol polyphosphate 1-phosphatase that hydrolyzes both inositol 1,3,4-trisphosphate (Ins-1,3,4-P3) and inositol 1,4-bisphosphate (Ins-1,4-P2), yielding inositol 3,4-bisphosphate and inositol 4-phosphate, respectively, as products (Inhorn, R. |
T3 |
106-408 |
Sentence |
denotes |
We recently identified an enzyme which we have designated inositol polyphosphate 1-phosphatase that hydrolyzes both inositol 1,3,4-trisphosphate (Ins-1,3,4-P3) and inositol 1,4-bisphosphate (Ins-1,4-P2), yielding inositol 3,4-bisphosphate and inositol 4-phosphate, respectively, as products (Inhorn, R. |
T4 |
409-457 |
Sentence |
denotes |
C., Bansal, V.S., and Majerus, P.W. (1987) Proc. |
T4 |
409-457 |
Sentence |
denotes |
C., Bansal, V.S., and Majerus, P.W. (1987) Proc. |
T5 |
458-463 |
Sentence |
denotes |
Natl. |
T5 |
458-463 |
Sentence |
denotes |
Natl. |
T6 |
464-469 |
Sentence |
denotes |
Acad. |
T6 |
464-469 |
Sentence |
denotes |
Acad. |
T7 |
470-474 |
Sentence |
denotes |
Sci. |
T7 |
470-474 |
Sentence |
denotes |
Sci. |
T8 |
475-481 |
Sentence |
denotes |
U.S.A. |
T8 |
475-481 |
Sentence |
denotes |
U.S.A. |
T9 |
482-497 |
Sentence |
denotes |
84, 2170-2174). |
T9 |
482-497 |
Sentence |
denotes |
84, 2170-2174). |
T10 |
498-598 |
Sentence |
denotes |
We have now purified the inositol polyphosphate 1-phosphatase 3600-fold from calf brain supernatant. |
T10 |
498-598 |
Sentence |
denotes |
We have now purified the inositol polyphosphate 1-phosphatase 3600-fold from calf brain supernatant. |
T11 |
599-763 |
Sentence |
denotes |
The purified enzyme has an apparent molecular mass of 44,000 daltons as determined by gel filtration and is free of other inositol phosphate phosphatase activities. |
T11 |
599-763 |
Sentence |
denotes |
The purified enzyme has an apparent molecular mass of 44,000 daltons as determined by gel filtration and is free of other inositol phosphate phosphatase activities. |
T12 |
764-924 |
Sentence |
denotes |
The enzyme hydrolyzes Ins-1,4-P2 with an apparent Km of approximately 4-5 microM, while it degrades Ins-1,3,4-P3 with an apparent Km of approximately 20 microM. |
T12 |
764-924 |
Sentence |
denotes |
The enzyme hydrolyzes Ins-1,4-P2 with an apparent Km of approximately 4-5 microM, while it degrades Ins-1,3,4-P3 with an apparent Km of approximately 20 microM. |
T13 |
925-1007 |
Sentence |
denotes |
The enzyme hydrolyzes these substrates at approximately the same maximal velocity. |
T13 |
925-1007 |
Sentence |
denotes |
The enzyme hydrolyzes these substrates at approximately the same maximal velocity. |
T14 |
1008-1144 |
Sentence |
denotes |
Inositol polyphosphate 1-phosphatase shows a sigmoidal dependence upon magnesium ion, with 0.3 mM Mg2+ causing half-maximal stimulation. |
T14 |
1008-1144 |
Sentence |
denotes |
Inositol polyphosphate 1-phosphatase shows a sigmoidal dependence upon magnesium ion, with 0.3 mM Mg2+ causing half-maximal stimulation. |
T15 |
1145-1261 |
Sentence |
denotes |
A Hill plot of the data is linear with a value of n = 1.9, suggesting that the enzyme binds magnesium cooperatively. |
T15 |
1145-1261 |
Sentence |
denotes |
A Hill plot of the data is linear with a value of n = 1.9, suggesting that the enzyme binds magnesium cooperatively. |
T16 |
1262-1355 |
Sentence |
denotes |
Calcium and manganese inhibit enzyme activity, with 50% inhibition at approximately 6 microM. |
T16 |
1262-1355 |
Sentence |
denotes |
Calcium and manganese inhibit enzyme activity, with 50% inhibition at approximately 6 microM. |
T17 |
1356-1443 |
Sentence |
denotes |
Lithium inhibits Ins-1,4-P2 hydrolysis uncompetitively with a Ki of approximately 6 mM. |
T17 |
1356-1443 |
Sentence |
denotes |
Lithium inhibits Ins-1,4-P2 hydrolysis uncompetitively with a Ki of approximately 6 mM. |
T18 |
1444-1646 |
Sentence |
denotes |
This mechanism of lithium inhibition is similar to that observed for the inositol monophosphate phosphatase (originally designated myo-inositol-1-phosphatase; Hallcher, L.M., and Sherman, W.R. (1980) J. |
T18 |
1444-1646 |
Sentence |
denotes |
This mechanism of lithium inhibition is similar to that observed for the inositol monophosphate phosphatase (originally designated myo-inositol-1-phosphatase; Hallcher, L.M., and Sherman, W.R. (1980) J. |
T19 |
1647-1652 |
Sentence |
denotes |
Biol. |
T19 |
1647-1652 |
Sentence |
denotes |
Biol. |
T20 |
1653-1658 |
Sentence |
denotes |
Chem. |
T20 |
1653-1658 |
Sentence |
denotes |
Chem. |
T21 |
1659-1724 |
Sentence |
denotes |
255, 10896-10901), suggesting that these two enzymes are related. |
T21 |
1659-1724 |
Sentence |
denotes |
255, 10896-10901), suggesting that these two enzymes are related. |
T22 |
1725-1804 |
Sentence |
denotes |
Lithium also inhibits Ins-1,3,4-P3 hydrolysis with an estimated Ki of 0.5-1 mM. |
T22 |
1725-1804 |
Sentence |
denotes |
Lithium also inhibits Ins-1,3,4-P3 hydrolysis with an estimated Ki of 0.5-1 mM. |