Expression in HEK293 cells, purification, and characterization of recombinant human α-glucosidases.

IF 1.4 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Bioscience, Biotechnology, and Biochemistry Pub Date : 2025-04-16 DOI:10.1093/bbb/zbaf055

So Nishimoto, Teisuke Takita, Kazumichi M Nishida, Masaaki Ito, Toshiyuki Kimura, Yasuhisa Kimura, Noriyuki Kioka, Kiyoshi Yasukawa

引用次数: 0

Abstract

In mammals, intestinal α-glucosidase exists within maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) complexes. Here, we purified recombinant human MGAM and SI from human embryonic kidney 293 (HEK293) cells using Flag tag-based affinity chromatography. Steady-state kinetic analysis at pH 6.0 and 37°C showed that the maltase activities of MGAM and SI were higher than their sucrase and isomaltase activities.

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重组人α-葡萄糖苷酶在HEK293细胞中的表达、纯化和表征。

哺乳动物肠道α-葡萄糖苷酶存在于麦芽糖酶-葡萄糖淀粉酶（MGAM）和蔗糖-异麦芽糖酶（SI）复合物中。在这里，我们使用基于Flag标签的亲和层析从人胚胎肾293 （HEK293）细胞中纯化重组人MGAM和SI。在pH 6.0和37℃的稳态动力学分析表明，MGAM和SI的麦芽糖酶活性高于蔗糖酶和异麦芽糖酶活性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Bioscience, Biotechnology, and Biochemistry 生物-生化与分子生物学

CiteScore

3.50

自引率

0.00%

发文量

183

审稿时长

1 months

期刊介绍： Bioscience, Biotechnology, and Biochemistry publishes high-quality papers providing chemical and biological analyses of vital phenomena exhibited by animals, plants, and microorganisms, the chemical structures and functions of their products, and related matters. The Journal plays a major role in communicating to a global audience outstanding basic and applied research in all fields subsumed by the Japan Society for Bioscience, Biotechnology, and Agrochemistry (JSBBA).