Matsumoto T, Yamaura I, Funatsu M
a Department of Applied Microbial Technology , The Kumamoto Institute of Technology , Kumamoto 860 , Japan.
Biosci Biotechnol Biochem. 1996 Jan;60(5):889-90. doi: 10.1271/bbb.60.889.
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.
南瓜谷氨酸脱羧酶先通过DEAE-纤维素分批法进行纯化，随后依次采用蓝色琼脂糖凝胶、纤维素精细GCL-2000和Toyopearl HW-55F柱色谱法进行纯化。纯化后的谷氨酸脱羧酶具有较高的比活性（95.0 u/mg）。谷氨酸脱羧酶的吸收光谱在300 - 500 nm范围内，于420 nm处有最大吸收峰。pH值从5.3变为7.8时，420 nm处的吸光度降低。1摩尔谷氨酸脱羧酶在pH 5.8和pH 7.8时分别含有3.8摩尔和1.3摩尔的磷酸吡哆醛。
