|
|
| type |
Journal Article |
| authors |
Kaisaki, P.J.; Jerkins, A.A.; Goodspeed, D.C.; Steele, R.D.; Kaisakia, P.J.
|
| title |
Cloning and characterization of rat cysteine sulfinic acid decarboxylase |
| journal |
Biochim Biophys Acta |
| Activity |
4.1.1.29 |
| sel |
unselected |
| ui |
yyyoooppp |
| year |
(1995) |
| volume |
1262 |
| number |
1 |
| pages |
79-82 |
| | |
|---|
| abstract |
Cysteine sulfinic acid decarboxylase (CSAD) is a key enzyme in taurine biosynthesis. CSAD activity and enzyme protein concentration are both repressed by the action of the steroid family hormones triiodothyronine and estrogen. To characterize this suppression, a cDNA clone for CSAD was isolated from a rat liver cDNA expression library using polyclonal antibodies to CSAD. The cDNA was sequenced in its entirety and confirmed to be a clone of CSAD. In a Northern blot comparing liver and kidney RNA of male and female rats, the CSAD cDNA probe detected a 2.5 kb mRNA band which was present at levels corresponding to the concentration of enzyme protein. Hyperthyroidism decreased CSAD mRNA as compared to euthyroid controls, providing evidence that negative regulation of CSAD activity occurs at the level of mRNA. -!-Erratum in: Biochim Biophys Acta 1995 Aug 22;1263(2):179. |
| last changed |
2004/03/25 11:09 |
|
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