人肝脏中1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶的纯化及某些性质
Purification and some properties of 1-aspartamido-beta-N-acetylglucosamine amidohydrolase from human liver.
作者信息
Dugal B, Stromme J
出版信息
Biochem J. 1977 Sep 1;165(3):497-502. doi: 10.1042/bj1650497.
Abstract
Human liver 1-aspartamido-beta-N-acetylglucosamine amidohydrolase (aspartylglucosylaminase, EC 3.5.1.26) was purified 17 500-fold to apparent homogeneity as judged from polyacrylamide-gel disc electrophoresis. A pH optimum of 7.7-9.0 was found. The Km value was pH- and temperature-dependent. At 37 degrees C and pH 7.7, Km was 0.16 mM and it increased to 0.29 at pH 6.0 and 0.23 at pH 9.0. At 25 degrees C and pH 7.7, a Km value of 0.99 mM was obtained. When the substrate concentration was varied, apparent Michaelis-Menten kinetics were obtained. p-Hydroxymercuribenzoate, glutathione or cysteine had no effect on the enzyme activity; 5 mM-N-acetylcysteine inhibited about 47% of the total enzyme activity. Apart from Cu2+, other bivalent ions were virtually ineffective at 1 mM. The kinetic study differentiates this enzyme from aspartylglucosylaminase from other sources.
摘要
人肝脏1-天冬氨酰-β-N-乙酰葡糖胺酰胺水解酶（天冬氨酰葡糖胺酶，EC 3.5.1.26）经纯化后，从聚丙烯酰胺凝胶圆盘电泳判断，其纯度提高了17500倍，达到了表观均一性。发现最适pH值为7.7 - 9.0。Km值受pH值和温度影响。在37℃和pH 7.7时，Km为0.16 mM，在pH 6.0时增加到0.29，在pH 9.0时为0.23。在25℃和pH 7.7时，Km值为0.99 mM。当底物浓度变化时，呈现出明显的米氏动力学。对羟基汞苯甲酸、谷胱甘肽或半胱氨酸对酶活性无影响；5 mM - N - 乙酰半胱氨酸抑制约47%的总酶活性。除Cu2+外，其他二价离子在1 mM时几乎无作用。动力学研究将该酶与其他来源的天冬氨酰葡糖胺酶区分开来。
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