Primary structure of monkey osteocalcin

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Abstract
The complete 49-residue amino acid sequence of osteocalcin from the old world monkey M. fascicularis was determined by efficient combination of gas chromatography-mass spectrometry and Edman techniques. This vitamin K dependent protein of bone matrix contains 3 .gamma.-carboxyglutamic acid residues at positions 17, 21 and 24, as well as a disulfide-bonded loop (23-29). Features of the sequence which apparently are required for the binding of Ca2+ were strongly conserved throughout evolution.