VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Isolation, various physico-chemical and catalytic properties of L-methionine-gamma-lyase from Pseudomonas taetrolens

   
Zanin V.A., Lukina V.I., Berezov T.T.
PubMed Id: 2815686
Year: 1989  Volume: 35  Issue: 4  Pages: 84-89
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.
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Zanin, V. A., Lukina, V. I., Berezov, T. T. (1989). Isolation, various physico-chemical and catalytic properties of L-methionine-gamma-lyase from Pseudomonas taetrolens. Voprosy Meditsinskoi Khimii, 35(4), 84-89.
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