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Characterization of iron incorporation into ferritin by ceruloplasmin.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Characterization of iron incorporation into ferritin by ceruloplasmin./
Author:	Juan, Shu-Hui.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 1998,
Description:	233 p.
Notes:	Source: Dissertations Abstracts International, Volume: 61-01, Section: B.
Contained By:	Dissertations Abstracts International61-01B.
Subject:	Biochemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9926526
ISBN:	9780599262706

Characterization of iron incorporation into ferritin by ceruloplasmin.
Juan, Shu-Hui.

Characterization of iron incorporation into ferritin by ceruloplasmin. - Ann Arbor : ProQuest Dissertations & Theses, 1998 - 233 p.

Source: Dissertations Abstracts International, Volume: 61-01, Section: B.

Thesis (Ph.D.)--Utah State University, 1998.

This item must not be sold to any third party vendors.

The research presented in this dissertation has focused on the characterization of iron incorporation and nucleation into the iron storage protein ferritin by ceruloplasmin. It was found that only the H chain of ferritin interacts with ceruloplasmin and stimulates its ferroxidase activity. One molar ratio of H chain to ceruloplasmin gave optimal iron loading. Excess ceruloplasmin resulted in iron oxidized but not loaded into ferritin. The extent of iron loading into ferritin by ceruloplasmin was decreased in the presence of two synthetic peptides, of which His and Met are ligands for copper in ceruloplasmin. Fluorescence intensity of these decapeptides was decreased upon the addition of ferritin, suggesting an interaction between decapeptides and ferritin. Two synthetic peptides, corresponding to the BC loop of the H and L chains, respectively, were utilized to investigate their effects on the ferroxidase activity of ceruloplasmin and on iron loading into ferritin by ceruloplasmin. Only the BC loop of the H chain stimulated the ferroxidase activity of ceruloplasmin and decreased the extent of iron loading into ferritin by ceruloplasmin. A mutant L chain with the BC loop of the H chain resulted in an increased initial rate of iron oxidation and iron loading by ceruloplasmin. Additionally, amino acid residues such as Tyr29 and Tyr34 in the H chain adjacent to the iron loading channel were found to serve as ligands for iron incorporated into the ferritin core. The number of putative nucleation sites in a recombinant ferritin H chain homopolymer altered by site-directed mutagenesis did not affect the maximal extent of iron incorporation, approximately 2,200 atoms of iron per ferritin. The number of putative nucleation sites in ferritin did affect the stability of the iron core of ferritin. Rat ferritin heteropolymers isolated from different tissues and fractionated according to their iron contents or subunit compositions showed that their iron content was independent of their subunit compositions and the amounts of iron and phosphate fit the equation [Fe] = 4404 − 5.61[Pi], which we published earlier. These results were also supported using recombinant rat liver ferritin heteropolymers with vastly different ratios of H to L chains, reconstituted by ceruloplasmin and incubation with phosphate.

ISBN: 9780599262706Subjects--Topical Terms:

518028
Biochemistry.
Subjects--Index Terms:

Ceruloplasmin

Characterization of iron incorporation into ferritin by ceruloplasmin.
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100 1 $a Juan, Shu-Hui. $3 3683556
245 1 0 $a Characterization of iron incorporation into ferritin by ceruloplasmin.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 1998
300 $a 233 p.
500 $a Source: Dissertations Abstracts International, Volume: 61-01, Section: B.
500 $a Publisher info.: Dissertation/Thesis.
500 $a Advisor: Aust, Steven D.
502 $a Thesis (Ph.D.)--Utah State University, 1998.
506 $a This item must not be sold to any third party vendors.
506 $a This item must not be added to any third party search indexes.
520 $a The research presented in this dissertation has focused on the characterization of iron incorporation and nucleation into the iron storage protein ferritin by ceruloplasmin. It was found that only the H chain of ferritin interacts with ceruloplasmin and stimulates its ferroxidase activity. One molar ratio of H chain to ceruloplasmin gave optimal iron loading. Excess ceruloplasmin resulted in iron oxidized but not loaded into ferritin. The extent of iron loading into ferritin by ceruloplasmin was decreased in the presence of two synthetic peptides, of which His and Met are ligands for copper in ceruloplasmin. Fluorescence intensity of these decapeptides was decreased upon the addition of ferritin, suggesting an interaction between decapeptides and ferritin. Two synthetic peptides, corresponding to the BC loop of the H and L chains, respectively, were utilized to investigate their effects on the ferroxidase activity of ceruloplasmin and on iron loading into ferritin by ceruloplasmin. Only the BC loop of the H chain stimulated the ferroxidase activity of ceruloplasmin and decreased the extent of iron loading into ferritin by ceruloplasmin. A mutant L chain with the BC loop of the H chain resulted in an increased initial rate of iron oxidation and iron loading by ceruloplasmin. Additionally, amino acid residues such as Tyr29 and Tyr34 in the H chain adjacent to the iron loading channel were found to serve as ligands for iron incorporated into the ferritin core. The number of putative nucleation sites in a recombinant ferritin H chain homopolymer altered by site-directed mutagenesis did not affect the maximal extent of iron incorporation, approximately 2,200 atoms of iron per ferritin. The number of putative nucleation sites in ferritin did affect the stability of the iron core of ferritin. Rat ferritin heteropolymers isolated from different tissues and fractionated according to their iron contents or subunit compositions showed that their iron content was independent of their subunit compositions and the amounts of iron and phosphate fit the equation [Fe] = 4404 − 5.61[Pi], which we published earlier. These results were also supported using recombinant rat liver ferritin heteropolymers with vastly different ratios of H to L chains, reconstituted by ceruloplasmin and incubation with phosphate.
590 $a School code: 0241.
650 4 $a Biochemistry. $3 518028
650 4 $a Molecular biology. $3 517296
650 4 $a Toxicology. $3 556884
653 $a Ceruloplasmin
653 $a Ferritin
653 $a Iron incorporation
653 $a Putative nucleation
690 $a 0487
690 $a 0307
690 $a 0383
710 2 $a Utah State University. $3 960049
773 0 $t Dissertations Abstracts International $g 61-01B.
790 $a 0241
791 $a Ph.D.
792 $a 1998
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9926526