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Title
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Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2.
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Authors
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G.Wagner,
D.Neuhaus,
E.Wörgötter,
M.Vasák,
J.H.Kägi,
K.Wüthrich.
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Ref.
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Eur J Biochem, 1986,
157,
275-289.
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PubMed id
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Abstract
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The complete sequence-specific assignment of the 1H nuclear magnetic resonance
spectrum of a major subform of rabbit liver metallothionein-2 is presented. The
sequential assignment procedures revealed a number of differences with regard to
results obtained by earlier partial chemical sequencing of a preparation now
known to be microheterogeneous. In particular, the present data indicate a
polypeptide chain length of 62 amino acid residues as compared to the occurrence
of 61 amino acids in all other known mammalian metallothioneins. In the new
sequence, which was also fully confirmed by chemical means, the additional amino
acid residue was identified as Ala8' inserted between Ala8 and Ala9 of the
standard amino acid numeration. In addition to the predominant protein species
all preparations contained a minor component, for which the two-dimensional
1H-nuclear magnetic resonance features are compatible with a chemically
different, homologous metallothionein.
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