|
type |
Journal Article |
authors |
Tang, X. W.; Hsu, C. C.; Sun, Y.; Wu, E.; Yang, C. Y.; Wu, J. Y. |
title |
Multiplicity of Brain Cysteine Sulfinic Acid Decarboxylase - Purification, Characterization and Subunit Structure |
journal |
J Biomed Sci |
Activity |
4.1.1.29 |
ui |
0; MBCSDPC |
year |
(1996) |
volume |
3 |
number |
6 |
pages |
442-453. |
| |
abstract |
Cysteine sulfinic acid decarboxylase (CSAD), the rate-limiting enzyme in taurine biosynthesis, appears to be present in the brain in multiple isoforms. Two distinct forms of CSAD, referred to as CSAD I and CSAD II, were obtained on Sephadex G-100 column. CSAD I and CSAD II differ in: (1) the elution profile on Sephadex G-100 column; (2) the sensitivity towards Mn(2+), methione, and other sulfur-containing amino acids, and (3) their immunologic properties. CSAD II has been purified to about 2,500-fold by a combination of column chromatographies and polyacrylamide gel electrophoresis (PAGE). The purity of the enzyme preparation was established as judged from the following observations: (1) a single protein band was observed under various electrophoretic conditions, e.g., 5-20% nondenaturing PAGE, 7% nondenaturing PAGE and 10% SDS-PAGE, and (2) in nondenaturing PAGE, the protein band comigrated with CSAD activity. CSAD II has a molecular weight of 90 kDa and is a homodimer consisting of two 43 +/- 2 kDa subunits. CSAD appears to require Mn(2+) for its maximum activity. Other divalent cations fail to replace Mn(2+) in activation of CSAD activity. However, the precise role of Mn(2+) in the action of CSAD remains to be determined. |
last changed |
2008/01/29 17:57 |
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