Affinity Chromatographic Purification and Characterization of Sialic Acid Binding Proteins in Bovine Kidney

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概要

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• Sialic acid binding proteins were purified from bovine kidney by successive affinity chromatography on fetuin and heparin clumns. The proteins adsorbed calcium-dependently on fetuin-Sepharose were further subjected to affinity chromatography on heparin-Sepharose. The proteins were separated into two fractions, fraction I and fraction II, by elution with 2mM EDTA and 0.3M NaCl, respectively. The affinity purified fractions had the binding activities to biotinylated fetuin in a polystyrene microtiter well, but not hemagglutinating activities. Inhibition assay of the binding revealed that N-acetylneuraminic acid is the most potent inhibitor for both fractions among the monosaccharides tested. Upon SDS-polyacrylamide gel electrophoresis, fraction-I gave three bands corresponding to 37kDa, 43kDa and 50kDa proteins and fraction-II four bands corresponding to 38kDa, 39kDa, 41kDa and 74kDa proteins. The proteins were electroblotted onto a polyvinylidene difluoride membrane and then subjected to the direct chemical analyses and the binding studies using horseradish peroxidase (HRP)-labeled binding probes. All the proteins had similar amino acid compositions and were N-terminally blocked. Neither of all proteins was stained with HRP-concanavalin A and HRP-peanut agglutinin, suggesting that they are not glycosylated. All of them were stained with HRP-fetuin and HRP-anhydrotrypsin. The results suggest that they have the carbohydrate recognition domain specific to N-acetylneuraminic acid and are the fragments produced by proteolytic digestion with endogenous trypsin family proteases in the kidney.

• お茶の水女子大学の論文

著者

• Matsumoto I

  お茶の水女子大学

• Matsumoto Isamu

  The Graduate School Of Humanities And Sciences Ochanomizu University

• Kojima K

  Kyushu Univ. Fukuoka

• OGAWA Haruko

  Department of Chemistry, Faculty of Science, Ochanomizu University

• Kojima Kyoko

  From the Department of Chemistry, Faculty of Science, Ochanomizu University

• Adachi Masami

  From the Department of Chemistry, Faculty of Science, Ochanomizu University

• Ogawa Haruko

  From the Department of Chemistry, Faculty of Science, Ochanomizu University

• Seno Nobuko

  From the Department of Chemistry, Faculty of Science, Ochanomizu University

• Matsumoto Isamu

  From the Department of Chemistry, Faculty of Science, Ochanomizu University

• Seno Nobuko

  From The Department Of Chemistry Faculty Of Science Ochanomizu University

• Ogawa Haruko

  Department Of Chemistry Faculty Of Science Ochanomizu University

• Ogawa Haruko

  Department Of Advanced Biosciences Graduate School Of Humanities And Sciences Ochanomizu University

• Kojima K

  Graduate School Of Pharmaceutical Sciences Nagoya City University

• Adachi Masami

  From The Department Of Chemistry Faculty Of Science Ochanomizu University

• Matsumoto I

  Ochanomizu Univ. Tokyo

• Matsumoto Isamu

  Matsumoto Institute Of Life Science

• Matsumoto Isamu

  Division Of Human Genetics Medical Research Institute Kanazawa Medical University

• Matsumoto Isamu

  Department Of Chemistry Faculty Of Science Ochanomizu University

• Matsumoto Isamu

  Graduate School Of Humanities And Sciences Ochanomizu University

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