Purification and Amino-acid-sequence of Human Motilin Isolated From a Motilin Containing Liver Metastasis

Declercq, P.;Deprez, Pierre;Vandermeers, A.;Vanassche, G.;Peeters, T.;et.al.
(1995) Regulatory Peptides — Vol. 55, n° 1, p. 79-84 (1995)

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Authors
  • Declercq, P.
    Author
  • Author
  • Vandermeers, A.
    Author
  • Vanassche, G.
    Author
  • Fiasse, RenéUCLouvain
    Author
  • Peeters, T.
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Abstract
The acid extract of a liver metastasis from a patient with elevated plasma motilin levels contained large quantities of motilin (3.37 mu g/ml). The extract was concentrated on a C-18-column and motilin was isolated by gel chromatography (Sephadex G-50) followed by cation ion exchange chromatography (RR5/5 Mono-S) and three successive steps of reverse phase chromatography (Nucleosil 300-5 C-18). The pure peptide was sequenced and the identity of porcine and human motilin was confirmed. This is the first report of a tumor containing large amounts of motilin.
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Citations

Declercq, P., Deprez, P., Vandermeers, A., Vanassche, G., Fiasse, R., Depoortere, I., Vandermeerspiret, MC., & Peeters, T. (1995). Purification and Amino-acid-sequence of Human Motilin Isolated From a Motilin Containing Liver Metastasis. Regulatory Peptides, 55(1), 79-84. https://doi.org/10.1016/0167-0115(94)00094-E (Original work published 1995)