J. Biol. Chem., Vol. 261, Issue 23, 10569-10575, Aug, 1986
Purification and characterization of chymodenin. A hormone-like peptide from porcine duodenum
JW Adelson, L Nelbach, GB Yates, A Ehrlich, CB Glaser and R Chang
Chymodenin, a hormone-like duodenal peptide which rapidly alters the
proportions of secreted pancreatic digestive enzymes to a mixture
relatively richer in chymotrypsinogen than that found in basal secretion,
has been purified to homogeneity. The starting material was an acidic
methanol-soluble, neutral pH-insoluble fraction of an acetic acid extract
of porcine duodenum; the purification consisted of cation- exchange
chromatography on SP-Sephadex and CM-Sephadex in ammonium bicarbonate
gradients, and gel filtration on Sephadex G-75 in dilute acetic acid. The
yield of material was followed by radioimmunoassay. Homogeneity was
determined from chymodenin's behavior in disc gel electrophoresis in an
acidic counter-migration-of-dye system, sodium dodecyl sulfate-urea gels,
gel filtration, dansyl-Edman reaction, reversed-phase high pressure liquid
chromatography, isotachophoresis, and sedimentation equilibrium
ultracentrifugation. The electrophoretic mobility, the molecular weight of
9,000-10,000, and the biological activity differed from those of other
gastrointestinal peptide hormones. The amino acid composition was unique.
Chymodenin is the first purified hormone-like substance reported capable of
altering the composition of the mixture of secreted digestive enzymes,
independent of the stimulation of massive pancreatic protein output.
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