ABSTRACT
An unknown amino acid was purified from bovine ligament elastin. The compound was shown by proton NMR to have a pyridinium ring structure similar to isodesmosine, yet containing an olefinic double bond on one additional side chain which was not attached to the pyridinium ring. Mass spectral analysis confirmed the NMR data and indicated a parent compound with a mass of 653. A structure is proposed that is derived from the condensation of five lysine residues. The trivial name of pentasine is proposed for this compound.
Subject(s)
Amino Acids/isolation & purification , Elastin/analysis , Animals , Cattle , Isodesmosine/analogs & derivatives , Ligaments/analysis , Lysine/analogs & derivatives , Magnetic Resonance Spectroscopy , Mass SpectrometryABSTRACT
Methods are described for the preparation of [8,9-2H2]apomorphine and [1,3,8,9-2H4]apomorphine based on reaction of apomorphine in trifluoroacetic acid-d. The mass spectral properties of these compounds and of the O,O-bis(heptafluorobutyrate) ester and the O,O-bis(tert-butyldimethylsilyl) ethers of apomorphine, using electron impact and chemical ionization, are reported. [1,3,8,9-2H4]Apomorphine was used to elaborate the 13C-NMR chemical shifts of the proton-bearing carbons of apomorphine.
