Premium
Menschliches Calcitonin. III. Struktur von Calcitonin M und D
Author(s) -
Neher R.,
Riniker B.,
Rittel W.,
Zuber H.
Publication year - 1968
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19680510811
Subject(s) - chemistry , calcitonin , antiparallel (mathematics) , dimer , stereochemistry , amino acid , arginine , amide , biochemistry , endocrinology , organic chemistry , medicine , physics , quantum mechanics , magnetic field
Abstract Human calcitonin M and its dimer calcitonin D, two highly active peptides isolated from C cell tumours, were subjected to sequence studies using chemical and enzymatic methods. For calcitonin M, containing 32 amino acid residues, the following structure was derived:Though the disulphide bridge between position 1 and 7, and the C‐terminal proline amide of human calcitonin M are the same as in porcine α‐thyrocalcitonin, many amino acid residues ‐ 18 in all ‐ are different throughout the molecule. Arginine and tryptophan are absent; on the other hand, lysine and isoleucine are to be found at position 18 and 27 respectively. Methionine changes its place from position 25 to 8 adjacent to the disulphide bridge. Experimental evidence indicates that calcitonin D represents the antiparallel dimeer of calcitonin M.