Studies on the structure of sphingomyelinase. Amino acid composition and heterogeneity on isoelectric focusing.

@article{Jones1983StudiesOT,
  title={Studies on the structure of sphingomyelinase. Amino acid composition and heterogeneity on isoelectric focusing.},
  author={Christopher Stephen Jones and Prema Shankaran and Dr. R. J. L. Davidson and Arthur T. Poulos and John William Callahan},
  journal={The Biochemical journal},
  year={1983},
  volume={209 2},
  pages={
          291-7
        }
}
Sphingomyelinase, purified to apparent homogeneity from human placenta, is an acidic protein, as judged from its amino acid composition and by isoelectric focusing of the carboxymethylated protein. The amino acid composition is characterized by an approximately equal content of hydrophobic and polar amino acid residues. The reduced-alkylated polypeptides were separated into two groups. Most of the polypeptides were heterogeneous with pI values of 4.4-5.0, but an additional more minor component… CONTINUE READING
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