Serum lipoproteins of sea bass (Dicentrarchus Labrax L.). Purification and partial characterization by density gradient ultracentrifugation and agarose column chromatography |
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Institution: | 1. University Strasbourg, INSERM U1109, MN3T (The Microenvironmental Niche in Tumorigenesis and Targeted Therapy), 3 avenue Molière, Strasbourg, Hautepierre, France;2. University Strasbourg, INSERM U1109, The Tumor Microenvironment Laboratory, Hôpital Civil, Institut d''Hématologie et d''Immunologie, Fédération de Médecine Translationnelle de Strasbourg (FMTS), 1 Place de l''Hôpital, 67091 Strasbourg, France;3. University Basel, Tumor Matrix laboratory, Department of Biomedicine, Mattenstrasse 57, Basel, Switzerland;4. Laboratoire des Venins et Molécules Thérapeutiques, Institut Pasteur Tunis, 13 Place Pasteur, BP74, 1002, Tunis, Tunisia;5. Medical School of Tunis, Tunis Université, Tunis, Tunisia;6. Institute for Dental Research and Oral Musculoskeletal Research, Center for Biochemistry, Center for Molecular Medicine Cologne (CMMC), Faculty of Medicine and University Hospital Cologne, University of Cologne, Joseph-Stelzmann-Str. 52, Cologne, Germany;7. Colzyx AB, Scheelevägen 2, 223 81 Lund, Sweden |
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Abstract: | - 1.1. Five classes of sea bass serum lipoproteins were purified by single vertical spin ultracentrifugation and agarose column chromatography
- 2.2. VLDL, beta migrating, are the larger and less dense lipoproteins.
- 3.3. LDL are the more heterogeneous in size, ranging from 11 × 106 to 1 × 106.
- 4.4. HDL represent the predominant class which, on the basis of density and electrophoresis migration, is differentiated in three subclasses.
- 5.5. VHDL float at a density > 1.22 mg/ml, which corresponds to the density of the other serum lipoproteins. This subclass, with an apparent molecular weight of 1.5 × 105, resembles the albumin-like fatty acids binding proteins, shown in mammals and teleosts and absent in elasmobranchs.
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