@article{oai:teapot.lib.ocha.ac.jp:00034795,
 author = {Matsumoto, Isamu and Jimbo, Akiko and Mizuno, Yuko and Seno, Nobuko and Jeanloz, Roger W.},
 issue = {1/2},
 journal = {お茶の水女子大學自然科學報告},
 month = {Dec},
 note = {application/pdf, 紀要論文, Potato lectin (Solanum tuberosum agglutinin, STA) was purified by affinity chromatography on (GlcNAc)_3-Sepharose 6B. The molecular weight of STA was estimated to be about 100,000 by gel filtration on Sephadex G-150 in 0.05M phosphate buffered saline, pH 7.2. By sedimentation equilibrium analysis, it was shown that STA was an aggregating system with a monomer molecular weight of 54,000. Equilibrium dialysis showed that STA (dimer) has two binding sites for a specific sugar per molecule. STA had a high content of sugar, most of which was arabinose, and was rich in Hyp and Cys. Upon interaction with specific sugars, STA induced a UV-difference spectrum having positive peaks at 292nm and 285nm, which seemed to be characteristic of the tryptophyl residue. The association constants of STA with chitin oligosaccharides were determined from the intensities of the difference spectra at various concentrations of sugars. They increased with increasing chain-length of the sugar. Frontal affinity chromatography of STA was performed on columns of immobilized chitin oligosaccharides and that of chitin oligosaccharides on a column\
 of immobilized STA. The association constants obtained with STA-Sepharose were in good agreement with those obtained by difference spectra, whereas those obtained with (GlcNAc)_2, 3-Sepharose were much higher, presumably owing to the effect of multivalency of ligands. The analyses of CD spectra of STA in the far UV region indicated the presence of approximately 40% of β and 60% of unordered form, and no evidence of α-helix conformation. This confirms the structure suggested by the unusual amino acid composition and by the high content of sugar.},
 pages = {55--75},
 title = {Studies on Solanum tuberosum Agglutinin},
 volume = {33},
 year = {1982}
}