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Improved Purification and Spectroscopic Properties of Squash Glutamate Decarboxylase
Author(s) -
Toshihiko Matsumoto,
Izumi Yamaura,
Masaru Funatsu
Publication year - 1996
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.60.889
Subject(s) - glutamate decarboxylase , chemistry , chromatography , cellulose , carboxy lyases , glutamate receptor , pyridoxal phosphate , absorption (acoustics) , squash , pyridoxal , biochemistry , nuclear chemistry , enzyme , biology , botany , materials science , cofactor , receptor , composite material
Squash glutamate decarboxylase was purified by DEAE-Cellulose batchwise followed by Blue-Sepharose, Cellulofine GCL-2000, and Toyopearl HW-55F column chromatography. The purified glutamate decarboxylase had a high specific activity (95.0 u/mg). The absorption spectrum of glutamate decarboxylase had an absorption maximum at 420 nm in the range 300-500 nm. A pH change from 5.3 to 7.8 was accompanied by a decrease in absorbancy at 420 nm. One mole of glutamate decarboxylase contained 3.8 and 1.3 mol of pyridoxal 5'-phosphate at pH 5.8 and pH 7.8, respectively.

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