| Autor: |
Zanin VA, Lukina VI, Berezov TT |
| Jazyk: |
ruština |
| Zdroj: |
Voprosy meditsinskoi khimii [Vopr Med Khim] 1989 Jul-Aug; Vol. 35 (4), pp. 84-9. |
| Abstrakt: |
Homogeneous preparation of L-methionine gamma-lyase was isolated from Ps. taetrolens. As shown by gel filtration and gradient polyacrylamide gel electrophoresis molecular mass of the native L-methionine gamma-lyase was 130-135 kDa. Polyacrylamide gel electrophoresis in presence of 0.1% SDS showed that L-methionine gamma-lyase proved to be a tetramer, which consisted of identical subunits with a molecular mass of 34 kDa. Pyridoxal-5'-phosphate was bound to the enzyme in the ratio of four moles of the cofactor per a mole of protein. The absorption spectrum of the enzyme exhibited maximal values at 420 nm, which is specific for a number of pyridoxal phosphate-containing enzymes. L-methionine gamma-lyase from Ps. taetrolens was found to be dissimilar in its physicochemical and catalytic properties to the same enzymes from other sources. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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