title: Partial characterization of peptide fragment purified by isoelectrofocusing after organo alkaline hydrolysis of bovine ligamentum nuchae elastin.
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.
mesh_terms: D000818:Animals; D002417:Cattle; D004549:Elastin / Q000032:analysis*; D006868:Hydrolysis; D007525:Isoelectric Focusing; D008022:Ligaments / Q000032:analysis*; D009333:Neck; D010455:Peptides / Q000302:isolation & purification*
chemical_list: D010455:Peptides; D004549:Elastin