J. Biol. Chem., Vol. 261, Issue 14, 6384-6389, May, 1986
Purification and primary sequences of the major arginine-containing antifreeze glycopeptides from the fish Eleginus gracilis
TS Burcham, DT Osuga, BN Rao, CA Bush and RE Feeney
An Arg-containing antifreeze glycoprotein from the polar fish Eleginus
gracilis was isolated, and the major components were purified to
homogeneity. The general protocol for purification was chromatography of
serum on DEAE-cellulose, followed by chromatography on a cation exchanger.
DEAE-cellulose chromatography resulted in two fractions, A and B. Fraction
A contained most of the antifreeze glycoprotein found in E. gracilis
(approximately 80% by weight) and consisted of 13 distinct components.
Unlike antifreeze glycoproteins from other previously studied polar fish,
Fraction A contained both low and high molecular weight antifreeze
glycoprotein components. The two major components of Fraction A were
sequenced and compared with the sequence of antifreeze glycoproteins 7 and
8 from both Boreogadus saida and Pagothenia borchgrevinki. The antifreeze
glycoproteins from E. gracilis were shown to have a similar composition to
those previously studied, except for an additional Ala-Arg dipeptide at the
carbon terminal in the major components of Fraction A and the position of
Pro in the low molecular weight components. The activity of E. gracilis
antifreeze glycoproteins is the subject of a companion article (Burcham, T.
S., Osuga, D. T., Yeh, Y., and Feeney, R. E. (1986) J. Biol. Chem. 261,
6390-6397).
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