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  • Title: Partial characterization of peptide fragment purified by isoelectrofocusing after organo alkaline hydrolysis of bovine ligamentum nuchae elastin.
    Author: Han KK, Davril M, Moczar M, Moczar E.
    Journal: Paroi Arterielle; 1981; 7(2):77-83. PubMed ID: 7322623.
    Abstract:
    Highly purified elastin from bovine ligamentum nuchae was submitted to partial alkaline hydrolysis (37 degree C, 72 H, 1 N KOH in 80 p. 100 aqueous ethanol). The non-coacervable fractions were submitted to isoelectrofocusing and five kappa-elastin fractions were obtained. The amino-acid compositions, the N-terminal amino-acids, the molecular weights and the thermolysin digests of each fraction were determined by various techniques. The average MW was about 14,500 (150 - 166 amino-acids). These results suggest that the distribution of cross-linking agents in fibrous elastin may not be uniform. The results also show that in certain cross-linked regions of similar molecular weight and size appearing to be composed of different polypeptides sequences containing different amounts of cross-links.
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