On ferritin heterogeneity. Further evidence for heteropolymers

Tissue ferritins from the horse, rat, and human consist of multiple isoferritins some of which are common to more than one tissue in the same individual. Subunit analyses indicate that the ferritins from all three species are similarly composed of only two types of subunit with an approximate Mr of...

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Bibliographic Details
Published in:The Journal of biological chemistry 1978-06, Vol.253 (12), p.4451-4458
Main Authors: Arosio, P, Adelman, T G, Drysdale, J W
Format: Article
Language:English
Subjects:
Amino Acids - analysis
Animals
Ferritins - biosynthesis
Horses
Humans
Liver - analysis
Macromolecular Substances
Molecular Weight
Myocardium - analysis
Peptide Fragments - analysis
Plants - metabolism
Protein Biosynthesis
Rats
Species Specificity
Spleen - analysis
Triticum - metabolism
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Summary:Tissue ferritins from the horse, rat, and human consist of multiple isoferritins some of which are common to more than one tissue in the same individual. Subunit analyses indicate that the ferritins from all three species are similarly composed of only two types of subunit with an approximate Mr of 21,000 and 19,000, designated H and L. The relative amounts of these subunits vary progressively throughout the isoferritin spectrum. Amino acid analyses and tryptic peptide maps indicate that the H and L subunits have extensive sequence homologies and that both are species-specific. Both subunits have been identified as the primary products of apoferritin synthesis in a wheat germ lysate programmed by rat liver mRNA. These results substantiate our proposal (Adelman, T. G., Arosio, P., and Drysdale, J. W. (1975) Biochem. Biophys. Res. Commun. 63, 1056-1062) that tissue ferritins are not unique homopolymers but families of hybrid molecules consisting of different proportions of two subunit types.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)34741-5