Abstract
THE two best known elastic proteins are elastin and resilin. So far, elastin has been, isolated only from vertebrates although the presence of elastin-like material has been reported in several invertebrates1,2. Resilin has been found only in arthropods3. Apart from their amino-acid composition, resilin and elastin differ in the way they are cross linked into three dimensional networks. Thus resilin contains di- and tri-tyrosine formed oxidatively from tyrosine residues4,5 and elastin contains desmosine and isodesmosine6 together with a small amount of lysinonorleucine7, all formed from lysine residues. The presence in foetal elastin of dityrosine has recently been reported8. During an investigation of elastic proteins from other phyla, I noticed that molluscan hinge ligaments contain phenolic compounds, which in several respects resemble dityrosine (Fig. 1). One of these compounds (compound A) has now been isolated and identified as 3,3′-methylene-bistyrosine (Fig. 2). The isolation procedure and the reasons for ascribing the structure in Fig. 2 to the compound are described in this communication; a more detailed description of the properties of the compound will be published later.
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ANDERSEN, S. Isolation of a New Type of Cross Link from the Hinge Ligament Protein of Molluscs. Nature 216, 1029–1030 (1967). https://doi.org/10.1038/2161029a0
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DOI: https://doi.org/10.1038/2161029a0
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