| RRC ID |
20799
|
| 著者 |
Kamo T, Shimogawara K, Fukuzawa H, Muto S, Miyachi S.
|
| タイトル |
Subunit constitution of carbonic anhydrase from Chlamydomonas reinhardtii.
|
| ジャーナル |
Eur J Biochem
|
| Abstract |
Carbonic anhydrase purified from the cell surface of Chlamydomonas reinhardtii was inactivated by treatment with dithiothreitol. This treatment caused dissociation of the holoenzyme into 35-kDa (A) and 4-kDa (B) subunits as revealed by SDS/PAGE. The 35-kDa subunit was further separated into two components A1 (35 kDa) and A2 (36.5 kDa) by SDS/PAGE using a gradient gel. These two components have the same amino acid sequence up to at least the 10th amino acid from the N-terminus. The molecular masses were estimated at 76 kDa and 35 kDa for the holoenzyme and the large subunit, respectively, and the molar ratio of the former to the latter at 1:2, by using the techniques of low-angle laser light-scattering photometry and precision differential refractometry combined with gel-filtration HPLC. The molar ratio of the 35-kDa/4-kDa subunits was estimated at 1:1 the gel-filtration HPLC monitored with precision differential refractometry. Atomic-absorption spectrophotometry revealed that the holoenzyme contains two atoms of zinc. These results suggest that the holoenzyme is a heterotetramer composed of two large subunits (A1 and A2) and two small subunits (B).
|
| 巻・号 |
192(2)
|
| ページ |
557-62
|
| 公開日 |
1990-9-11
|
| DOI |
10.1111/j.1432-1033.1990.tb19261.x
|
| PMID |
2120056
|
| MeSH |
Amino Acid Sequence
Animals
Carbonic Anhydrases / genetics*
Carbonic Anhydrases / isolation & purification
Cell Membrane / enzymology
Chlamydomonas / enzymology*
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
Humans
Macromolecular Substances
Molecular Sequence Data
Molecular Weight
Peptide Fragments / isolation & purification
Peptide Mapping
Sequence Homology, Nucleic Acid
|
| 引用数 |
44
|
|
WOS 分野
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| リソース情報 |
| 藻類 |
NIES-2235 |
