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Vopr Med Khim ; 35(4): 84-9, 1989.
Article in Russian | MEDLINE | ID: mdl-2815686

ABSTRACT

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.


Subject(s)
Carbon-Sulfur Lyases/isolation & purification , Lyases/isolation & purification , Pseudomonas/enzymology , Carbon-Sulfur Lyases/metabolism , Catalysis , Chromatography, Liquid , Electrophoresis, Polyacrylamide Gel , Spectrophotometry, Ultraviolet , Temperature
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