L-Tyrosine carboxy-lyase of barley roots |
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Authors: | HOSOI KAZUO; YOSHIDA SEIICHI; HASEGAWA MASAO |
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Institution: | Department of Biology, Tokyo Metropolitan University Fukazawa, Setagaya-ku, Tokyo, Japan |
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Abstract: | L-Tyrosine carboxy-lyase (E.C. 4. 1. 1. 25) was isolated fromroots of germinating barley (Hordeum vulgare). The enzyme requirespyridoxal phosphate for maximum activity. The optimum pH foractivity is about 7.0. The enzyme is inhibited by p-chloromercuribenzoateand hydroxylamine at 103 M. Enzyme activity is foundin extracts from young roots, especially from those in earlystages of development, but not in extracts from shoots of thesame plant. Localization and changes in the amounts of L-tyrosinecarboxy-lyase and aromatic amines in developing barley seedlingswere measured. Participation of carboxy-lyase in the formationof aromatic amines in barley roots is suggested. (Received July 17, 1970; ) |
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