HUMAN FERRITIN H-CHAINS CAN BE OBTAINED IN NONASSEMBLED STABLE FORMS WHICH HAVE FERROXIDASE ACTIVITY

被引：20

作者：

LEVI, S ^{[1
]}

SANTAMBROGIO, P ^{[1
]}

ALBERTINI, A ^{[1
]}

AROSIO, P ^{[1
]}

机构：

[1] UNIV BRESCIA, INST CHEM, BRESCIA, ITALY

来源：

FEBS LETTERS | 1993年 / 336卷 / 02期

关键词：

FERROXIDASE; FERRITIN; IRON PROTEIN; PROTEIN ASSEMBLY;

D O I：

10.1016/0014-5793(93)80826-G

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：

We found conditions to obtain the Leu-169 --> Arg mutant of human ferritin H chain in a stable and non-assembled state. The protein obtained is an oligomer of subunits with a high degree of structured conformation, and when concentrated it re-assembles into ferritin cages. Functional studies showed that (i) it promotes iron oxidation like the assembled ferritin, but at slower rate, (ii) it is readily precipitated by the oxidised iron unless apotransferrin or L-chain ferritin are added to sequester Fe(III). The results confirm that ferroxidase activity is located within the H-chain, and indicate that the cages of the fully assembled ferritins are important not only in maintaining iron in a soluble form, but also in eliciting the activity of the ferroxidase centres.

引用

页码：309 / 312

页数：4

共 14 条

[1] OVERPRODUCTION, PURIFICATION AND CHARACTERIZATION OF THE BACTERIOFERRITIN OF ESCHERICHIA-COLI AND A C-TERMINALLY EXTENDED VARIANT [J].