ISSN:
0018-019X
Keywords:
Chemistry
;
Organic Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
Two highly active calcitonin peptides, M with 32 amino acids, and D a dimer of M, were isolated from a large human mediastinal C cell tumour. D can easily be transformed into M by the action of 1N ammonia; D and M afford two different sulphoxides, but all four peptides yield the same product upon oxidation with performic acid. Both D and M have a potency of about 120 MRC units/mg dry weight; their sulphoxides, by contrast, are almost inactive. Tryptic digestion of M produces an N-terminal octadecapeptide (TrI) and a C-terminal tetradecapeptide (TrII), the latter being also obtained from D. Amino acid analysis and other analytical data are presented. The structure of the human calcitonin peptides D and M is thus very different from that of porcine α-thyrocalcitonin.
Additional Material:
1 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/hlca.19680510731
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