Purification and characterization of two soluble acid invertase isozymes from Japanese pear fruit

被引：31

作者：

Hashizume, H ^{[1
]}

Tanase, K ^{[1
]}

Shiratake, K ^{[1
]}

Mori, H ^{[1
]}

Yamaki, S ^{[1
]}

机构：

[1] Nagoya Univ, Grad Sch Bioagr Sci, Hort Sci Lab, Chikusa Ku, Nagoya, Aichi 4648601, Japan

来源：

PHYTOCHEMISTRY | 2003年 / 63卷 / 02期

关键词：

Japanese pear (Pyrus serotina) fruit; soluble acid invertase (AIV; EC 3.2.1.26); enzyme purification; isozymes of AIV;

D O I：

10.1016/S0031-9422(03)00107-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two isozymes (AIV I and AIV II) of soluble acid invertase (EC 3.2.1.26) were purified from Japanese pear fruit through procedures including (NH4)(2)SO4 precipitating, DEAE-Sephacel column chromatography, Concanavalin A (ConA)-Sepharose affinity chromatography, hydroxyapatite column chromatography and Mono Q HR 515 column chromatography. The specific activities of purified AIV I and AIV II were 2670 and 2340 (nkat/mg protein), respectively. AIV I was a monomeric enzyme of 80 kDa, while AIV II may be also a monomeric enzyme, which is easy to be cleaved to 52 kDa and 34 kDa polypeptide during preparation by SDS-PAGE. The Km values for sucrose of AIV I and AIV II were 3.33 and 4.58 mM, respectively, and optimum pH of both enzyme activities was pH 4.5. (C) 2003 Published by Elsevier Science Ltd.

引用

页码：125 / 129

页数：5

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