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小肠果糖-1,6-二磷酸酶。纯化及与肝脏和肌肉果糖-1,6-二磷酸酶的比较。

Fructose-1,6-biphosphatase of the small intestine. Purification and comparison with liver and muscle fructose-1,6-bisphosphatases.

作者信息

Mizunuma H, Tashima Y

出版信息

J Biochem. 1978 Aug;84(2):327-36. doi: 10.1093/oxfordjournals.jbchem.a132132.

Abstract

The occurrence of specific fructose-1,6-bisphosphatase [D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11] (Fru-1,6-P2ase) in the small intestine was confirmed. 1. Fru-1,6-P2ase was isolated from mouse small intestine by a simple method. The isolated enzyme preparation was an electrophoretically homogeneous protein. 2. The molecular weight and subunit molecular weight were 140,000 and 38,000, respectively. 3. The intestinal enzyme was electrophoretically distinct from the liver enzyme. 4. The kinetic properties of the purified intestinal enzyme were compared with those of the mouse liver and muscle enzymes. 5. Mouse intestinal and muscle Fru-1,6-P2ases hydrolyzed ribulose-1,5-bisphosphate in addition to fructose-1,6-bisphosphate and sedoheptulose-1,7-bisphosphate.

摘要

已证实在小肠中存在特异性果糖-1,6-二磷酸酶D-果糖-1,6-二磷酸1-磷酸水解酶,EC 3.1.3.11。1. 通过一种简单方法从小鼠小肠中分离出Fru-1,6-P2ase。分离得到的酶制剂是一种电泳纯的蛋白质。2. 其分子量和亚基分子量分别为140,000和38,000。3. 肠道酶在电泳上与肝脏酶不同。4. 将纯化的肠道酶的动力学特性与小鼠肝脏和肌肉酶的动力学特性进行了比较。5. 小鼠肠道和肌肉中的Fru-1,6-P2ase除了能水解果糖-1,6-二磷酸和景天庚酮糖-1,7-二磷酸外,还能水解核酮糖-1,5-二磷酸。

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