ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
Enzyme-purified elastin from bovine ligamentum nuchae was digested with elastase in the presence of sodium dodecyl sulfate. Chromatographic fractionation of the digest, after removal of the detergent, resulted in the high-yield isolation of two peptide fractions (F2 and F3) that differed in size and composition. The larger, F2, which accounted for about 55% of the starting material, was subjected to sedimentation-equilibrium analysis in three chaotropic solvents. Comparison of the distribution of point-average molecular weights (Mw and Mz) with protein concentration in the three systems lead to the conclusion that significant self-association of peptides occurred in the absence of 6M guanidinium hydrochloride. In this solvent, the molecular-weight distribution was between 25,000 and 34,000, a range of values in agreement with an intrinisic viscosity of 13.1 cc g-1 determined in the same solvent. Assessment of chain weight by N- and C-terminal analysis was consistent with F2 being a multichain molecule comprising four polypeptide chains linked by three polyfunctional amino acids. Results are interpreted in terms of an anisotropic ultrastructural model of the protein, in which four polypeptide chains constitute the primary filament visualized by electron microscopy in the intact fiber.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360240808
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