N-epsilon-acetylation of porcine mature erythrocytes ubiquitin |
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| Authors: | D X Zhu L X Xu N Z Zhu G Briand K K Han |
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| Affiliation: | 1. Department of Biochemistry, University of Nanjing, Hankou Road II, Nanjing, People''s Republic of China;2. Unité INSERM No. 16, Biochimie des Protéines, Place de Verdun, 59045 Lille Cédex, France[Tel. (20)97-26-15];1. Laboratory of Genetics, Salk Institute for Biological Studies, La Jolla, California, 92037, USA;2. Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California, 92037, USA;3. Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri, 63110, USA;1. Department of Cell Physiology and Molecular Biophysics and Center for Membrane Protein Research, Texas Tech University Health Sciences Center, 3601 4th Street STOP 6551, Lubbock, TX 79430, USA;2. Current address: Department of Biology, Texas State University, 601 University Drive, San Marcos, TX 78666, USA;1. Department of Natural Sciences, Novosibirsk State University, 630090 Novosibirsk, Russian Federation;2. V. V. Voevodsky Institute of Chemical Kinetics and Combustion, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russian Federation;3. A. V. Nikolaev Institute of Inorganic Chemistry, Siberian Branch of the Russian Academy of Sciences, 630090 Novosibirsk, Russian Federation;1. School of Basic Medical Science, Guizhou Medical University, Guiyang, Guizhou 550004 China;2. School of Pharmacy, Guizhou Medical University, Guiyang, Guizhou 550004 China;3. Engineering Research Center for the Development and Application of Ethnic Medicine and TCM, Ministry of Education, Guizhou Medical University, Guiyang, Guizhou 550004 China |
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| Abstract: | Highly purified of porcine mature erythrocytes ubiquitin were obtained according to the experimental procedure reported by Jabusch and Deutsch (1983). N-epsilon-acetylation in vitro of internal lysyl residues of ubiquitin by p-nitro-phenyl-acetate at pH 8.0 was performed. The extent of acetylation of ubiquitin was determined: about 4-5 residues (4.5 residues) of N-epsilon-lysine groups of ubiquitin were acetylated. We have assigned by Edman degradation the sites of acetylation and the sites of remaining free internal N-epsilon-lysine residues in the sequence: fully acetylated: Lys-6, Lys-11 and Lys-33. Partially free N-epsilon-lysine: Lys-27 and Lys-29 and probably Lys-48 and Lys-63. 50 cycles Edman degradation were performed on porcine ubiquitin and the first 45 N-terminal residues were identified. We have partially determined that the molecular conservation of 45 amino acid sequence of ubiquitin between cattle, man and swine since the 45 amino acid sequence out of 76 residues are identical. The amino acid composition between human and porcine ubiquitin are also identical. |
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