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  • 2S albumin  (1)
  • Amino acid sequence  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Ferritin subunits in livers of siderotic mice (1989)
    Springer
    BioMetals 2 (1989), S. 77-82 
    Details
    ISSN: 1572-8773
    Keywords: Ferritin ; Siderotic mice ; Amino acid sequence ; L subunit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The major ferritin species of mouse liver has been resolved by SDS-PAGE into two bands similar to the H and L subunits of rat liver ferritin with the L subunit predominating. Amino acid sequencing has confirmed the major, faster-migrating component as L chain. An additional, electrophoretically fast, minor ferritin was isolated from siderosome-containing subcellular fractions. In denaturing gels it gave a single ‘F’ subunit band of about 17 kDa, significantly smaller than the L and H subunits (about 20 and 21 kDa respectively). A small fragment isolated from the fast ferritin was sequenced. It corresponds to a 19-residue C-terminal peptide cleaved from L subunits in the assembled molecules. The F subunit must be derived from L subunits by loss of this peptide, and is not the expression product of a different gene. ‘Fast’ ferritins of siderotic mice and rats are thus analogous.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01129204
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Theinus communis2S albumin precursor: A single preproprotein may be processed into two different heterodimeric storage proteins (1990)
    Springer
    Molecular genetics and genomics 222 (1990), S. 400-408 
    Details
    ISSN: 1617-4623
    Keywords: Ricinus ; 2S albumin ; Preproprotein processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary TheRicinus communis (castor bean) 2S albumin is a heterodimer of glutamine-rich, disulphidelinked 4 and 7 kDa polypeptides. A cDNA library was constructed using mRNA from maturing castor bean endosperm as template. Clones containing sequences complementary to albumin mRNA were isolated by hybridization using as a probe a mixture of synthetic oligonucleotides representing sequences predicted for a peptide present in the 2 S albumin large subunit. The nucleotide sequence contained an open reading frame encoding a preproprotein of 258 amino acid residues. The preproprotein included both polypeptides of the previously sequenced 2S albumin. In addition, this precursor included two further glutamine-rich sequences which, in terms of their size and conserved cysteine residues typically found in seed proteins of the 2S albumin superfamily, possibly represent the small and large polypeptide subunits of a second heterodimeric storage protein. A post-translational processing scheme is proposed which would result in a single preproprotein generating two distinct heterodimeric 2S albumins. The generation of a second heterodimer seems likely since polypeptide candidates for its small and large subunits were found in theRicinus 2S albumin fraction, and N-terminal protein sequencing confirmed the existence of the putative small subunit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00633846
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    Paper (German National Licenses)
    Fulltext
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