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Clinical Research Group for Gastrointestinal Endocrinology of the Max-Planck-Gesellschaft at the University of Göttingen, D-3400 Göttingen, Federal Republic of Germany [J. M. C., G. P. M.]; Department of Surgery, Karolinska Hospital, Stockholm, Sweden [G. W.]; Department of Pathology, University Hospital, Uppsala, Sweden [L. G.]; and Novo Research Institute, Bagsvaerd, Denmark [L. T.]
Peptides synthesized by a human medullary thyroid carcinoma were purified to homogeneity by reverse-phase high performance liquid chromatography and structurally characterized by determination of amino acid composition, amino acid sequence, and fast atom bombardment mass spectra. The katacalcin-related material in the tumor extract was heterogeneous. Katacalcin (121) represented the predominant molecular form but metabolites, identified as katacalcin (120), (119), (115) and (113), were also identified in high concentration. Calcitonin gene-related peptide-I was isolated from the tumor but calcitonin gene-related peptide-II was absent. A minor component of calcitonin gene-related peptide-like immunoreactivity was of higher molecular weight and may represent an incompletely processed form of the prohormone. Gastrin-releasing peptide (127) and gastrin-releasing peptide (1827) (neuromedin C) were isolated from the tumor but gastrin-releasing peptide (1427) and bombesin were absent.
1 This work was supported by the Stiftung Volkswagenwerk and the Swedish Medical Research Council (Project 102).
2 To whom requests for reprints should be addressed, at Klinische Arbeitsgruppe der MPG, Gosslerstrasse 10D, D-3400 Göttingen, Federal Republic of Germany.
Received 6/ 2/87. Revised 10/30/87. Accepted 2/ 8/88.
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