Purification and characterization of phosphohexose isomerase from human gastrointestinal carcinoma and its potential relationship to neuroleukin.

@article{Baumann1988PurificationAC,
  title={Purification and characterization of phosphohexose isomerase from human gastrointestinal carcinoma and its potential relationship to neuroleukin.},
  author={Michael Baumann and Karsten Brand},
  journal={Cancer research},
  year={1988},
  volume={48 24 Pt 1},
  pages={7018-21}
}
Phosphohexose isomerase (PHI) derived from human gastrointestinal tumor tissue was isolated by specific elution from a cation exchanger. The identity of three PHI variants in the purified preparation could be demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing analysis. By preparative IEF the variants could be resolved to high homogeneity. The monomer of the common major variant with a pI of 9.1 revealed a molecular weight of 60,000, whereas for… CONTINUE READING
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