Lipid transfer protein from Manduca sexta hemolymph |
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| Authors: | R O Ryan M A Wells J H Law |
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| Affiliation: | 1. Department of Thoracic and Cardiovascular Surgery, Heart and Vascular Institute, Cleveland Clinic, Cleveland, Ohio;2. Department of Cardiovascular Medicine, Heart and Vascular Institute, Cleveland Clinic, Cleveland, Ohio;3. Department of Quantitative Health Sciences, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio;1. Chair of Soil Science, Technical University of Munich, Emil-Ramann-Strasse 2, 85354 Freising, Germany;2. CNRS, IEES (UMR 7618 UPMC-CNRS-UPEC-IRD) CentreAgroParisTech-INRA, bâtiment EGER, Thiverval-Grignon 78850, France;3. INRA, UMR 1402 INRA-AgroParisTech ECOSYS, Thiverval-Grignon 78850, France;4. Institute for Advanced Study, Technical University of Munich, 85748 Garching, Germany;1. Dept. of Civil and Environmental Engineering, School of Engineering, Univ. de Antioquia, Calle 67 # 53-108. A. A. 1226, Medellín, Colombia;2. Dept. of Civil and Environmental Engineering, University of Maine, Orono, ME, United States;3. Dept. of Civil Engineering, School of Engineering, National University of Colombia, Medellín, Colombia |
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| Abstract: | A hemolymph lipid transfer protein (LTP) was isolated from the tobacco hornworm, Manduca sexta. LTP catalyzes net lipid transfer between isolated hemolymph lipoproteins in vitro. An isolation procedure employing density gradient ultracentrifugation and gel permeation chromatography produced a purified protein. LTP is a very high density lipoprotein with a particle Mr greater than 500,000. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that LTP is comprised of two apoproteins: apoLTP-I (Mr approximately 320,000) and apoLTP-II (Mr approximately 85,000). LTP may have a physiological role in altering the lipid content and composition of the major hemolymph lipoprotein, lipophorin. |
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