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Sequence of the peptide component of low‐molecular‐weight chromium‐binding substance
Author(s) -
Vincent John B.,
Chen Yuan,
Watson Heather,
Cassady Carolyn J.
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.537.5
Subject(s) - peptide , chromium , chemistry , biomolecule , trifluoroacetic acid , transferrin , peptide sequence , amino acid , biochemistry , chromatography , organic chemistry , gene
Two biomolecules are known to bind chromium in the body: transferrin and low‐molecular‐weight chromium‐binding substance (LMWCr). While transferrin is responsible for the transfer of Cr from the bloodstream to the tissues, LMWCr has been proposed to have a function in the removal of chromium from the body and in the enhancement of insulin signaling. LMWCr is comprised of a peptide that can tightly bind four equivalents of Cr(III). While reports on the magnetic and spectroscopic properties of the chromic centers have appeared, research has been hampered by difficulties in characterizing the organic portion of the biomolecule. Treatment of LMWCr with trifluoroacetic acid releases the Cr, converts the amino terminal glutamate of the peptide to pyroglutamate, and generates a heptapeptide. This procedure has allowed the isolation of the chromium‐free peptide component of LMWCr from a variety of sources; this peptide can be sequenced by mass spectrometry.