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
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom