| Autor: |
S, Pavagi, S, Kochhar, V K, Kochhar, P V, Sane |
| Rok vydání: |
1995 |
| Předmět: |
|
| Zdroj: |
Biochemistry and molecular biology international. 36(3) |
| ISSN: |
1039-9712 |
| Popis: |
Homoserine dehydrogenase (HSDH) has been purified to homogeneity from spinach leaves using ammonium sulphate fractionation followed by ion exchange chromatography, gel filtration and FPLC techniques. The purified enzyme has a relative molecular mass of 220,000 and subunit molecular mass of 55,000 and probably occurs as a tetramer. The enzyme was found to be sensitive to threonine and also exhibited aspartate kinase (AK) activity, which was also sensitive to threonine suggesting that it is a bifunctional protein. The enzyme protein also gave a positive cross reaction with antibodies raised against purified AK isoenzymes. Both HSDH and AK activities were stimulated by calcium and calmodulin. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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