PARTIAL-PURIFICATION AND PROPERTIES OF GLUTATHIONE-PEROXIDASE FROM CARP HEPATOPANCREAS

被引：18

作者：

NAKANO, T

SATO, M

TAKEUCHI, M

机构：

[1] Laboratory of Marine Biochemistry, Department of Fishery Science, Faculty of Agriculture, Aoba-ku, Sendai

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1992年 / 102卷 / 01期

关键词：

D O I：

10.1016/0305-0491(92)90268-V

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：

1. Two glutathione peroxidases (GSH-Px), D1 and D2, were partially purified from the hepatopancreas of common carp Cyprinus carpio by ion-exchange, gel filtration, and hydrophobic chromatography. The enzymatic properties of those enzymes were examined. 2. The D1 and D2 differed in following enzymatic properties. The pH optima of D1 and D2 were 8.0 and 9.0, respectively. 3. When stored at pH 4.0 for 36 hr, D1 kept 70% of maximal activity while only 30% of that was shown in D2. 4. D1 and D2 lost activity by 50% when incubated at 55-degrees-C and 65-degrees-C for 10 min, respectively.

引用

页码：31 / 35

页数：5

共 18 条

[1]

ASADA K, 1978, PROTEIN NUCLEIC ACID, V23, P200

[2]

AWASTHI YC, 1975, J BIOL CHEM, V250, P5144

[3] RAINBOW-TROUT LIVER MICROSOMAL LIPID-PEROXIDATION - THE EFFECT OF PURIFIED GLUTATHIONE-PEROXIDASE, GLUTATHIONE S-TRANSFERASE AND OTHER FACTORS [J].