An x-ray small-angle-scattering study of the structure of trypsin treated low density lipoprotein from human serum. |
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Authors: | P Laggner M J Chapman S Goldstein |
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Affiliation: | 1. Institut für Röntgenfeinstrukturforschung der Österreichischen Akademie der Wissenschaften und des Forschungszentrums, Steyrergasse 17, A-8010 Graz, Austria.;2. Unité 35, Institut National de la Santé et de la Recherche Médicale, Hôpital Henri Mondor, 94010 Créteil, France. |
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Abstract: | X-ray small-angle-scattering curves were obtained from human serum low-density lipoprotein (LDL) from which some 20 % of the protein moiety had been removed by limited tryptic digestion, and the results are compared to those from the undigested lipoprotein. The basic structural features of LDL, i.e. a quasi-spherical shape and internal lipid compartmentation, were essentially unaltered by tryptic treatment. The trypsin-treated material exhibited the same thermotropic transition as the control. Our experiments indicate that proteolysis affected the outermost electrondense shell in a uniform manner, without causing any significant alterations in the radial symmetry of the internal molecular architecture. Since none of the structural regularities observed in the real-space pair distance distribution are affected, in particular the 3.6 nm periodicity below 15°C, it is concluded that these regularities do not relate to the protein arrangement in LDL. |
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Keywords: | LDL low density lipoprotein T-LDL partially trypsin digested LDL |
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