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Analysis of the binding of bovine and human fibrinogen to ferritin: evidence that fibrinogen is a co...

Analysis of the binding of bovine and human fibrinogen to ferritin: evidence that fibrinogen is a co...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1730068915

Analysis of the binding of bovine and human fibrinogen to ferritin: evidence that fibrinogen is a common ferritin-binding protein in mammals

About this item

Full title

Analysis of the binding of bovine and human fibrinogen to ferritin: evidence that fibrinogen is a common ferritin-binding protein in mammals

Publisher

Dordrecht: Springer Netherlands

Journal title

Biometals, 2015-08, Vol.28 (4), p.679-685

Language

English

Formats

Publication information

Publisher

Dordrecht: Springer Netherlands

More information

Scope and Contents

Contents

Both human and horse fibrinogen are heme-binding proteins, and horse fibrinogen also exhibits heme-mediated ferritin binding. This study found that bovine and human fibrinogen are heme-mediated ferritin-binding proteins and demonstrated direct binding of bovine ferritin to protoporphyrin (PPIX) and its derivatives or to Zn ions. Binding of bovine a...

Alternative Titles

Full title

Analysis of the binding of bovine and human fibrinogen to ferritin: evidence that fibrinogen is a common ferritin-binding protein in mammals

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_1730068915

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1730068915

Other Identifiers

ISSN

0966-0844

E-ISSN

1572-8773

DOI

10.1007/s10534-015-9853-9

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