@article{oai:teapot.lib.ocha.ac.jp:00034739,
 author = {Kojima, Kyoko and Adachi, Masami and Ogawa, Haruko and Seno, Nobuko and Matsumoto, Isamu},
 issue = {1},
 journal = {お茶の水女子大學自然科學報告},
 month = {Jul},
 note = {application/pdf, 紀要論文, 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.},
 pages = {1--11},
 title = {Affinity Chromatographic Purification and Characterization of Sialic Acid Binding Proteins in Bovine Kidney},
 volume = {42},
 year = {1991}
}