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Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and biology >
Vol.29 >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10466/3050

Title: Some Further Properties of the Partially Purified γ-Aminobutyrate Transaminase from Bacillus cereus Strain K-22
Authors: TOKUNAGA, Hiroko
TOKUNAGA, Masao
NAKANO, Yoshihisa
KITAOKA, Shozaburo
Keywords: GABA
γ-aminobutyric acid
PALP
pyridoxal-5'-phosphate
pCMB
p-chloro-mercuribenzoic acid
Issue Date: 31-Mar-1977
Publisher: University of Osaka Prefecture
Citation: Bulletin of the University of Osaka Prefecture. Ser. B, Agriculture and biology. 1977, 29, p.24-31
Abstract: GABA transaminase was purified about 70-fold over a crude extract of Bacillus cereus K-22 and the stoichiometries of the forward and reverse enzyme reactions were established. This enzyme required pyridoxal-5'-phosphate as a cofactor and the molecular weight of this enzyme was estimated to be 130,000 by gel filtration. This enzyme was inhibited by sulfhydryl inhibitor and the inhibition was restored by sulfhydryl compounds. The enzyme was more active and exhibited higher stability against heat treatment in the presence of sulfhydryl compounds.
URI: http://hdl.handle.net/10466/3050
Appears in Collections:Vol.29

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