PMID: 3758061Sep 1, 1986Paper

Isolation and characterization of a lectin from tulip bulbs, Tulipa gesneriana

European Journal of Biochemistry
Y Oda, K Minami

Abstract

A lectin, which agglutinated specifically the yeast cells of the Saccharomyces genus, was isolated from tulip bulbs (Tulipa gesneriana) using affinity chromatography on mannan-Sepharose 4B. Its relative molecular mass was determined by gel filtration to be approximately 67,000. On polyacrylamide gel electrophoresis in sodium dodecyl sulfate, a relative molecular mass of 17,000 was obtained, suggesting that the lectin is a tetramer. Binding studies performed with iodinated lectin indicated that Saccharomyces cerevisiae cells contained approximately 5.7 X 10(6) binding sites per cell, whereas little binding was observed with yeasts other than the Saccharomyces genus, bacteria and animal erythrocytes. D-Mannose, D-mannose 6-phosphate, L-fucose and L-fucosylamine were potent inhibitors of the lectin binding to S. cerevisiae cells, while, D-glucose, D-galactose and D-mannosamine were inactive, indicating that hydroxyl group at C-2 of D-mannose was essential for the lectin binding. Furthermore, inhibition experiments, using various manno-oligosaccharides, suggested that the lectin recognized (1----6)-linked manno-oligosaccharide units larger than mannobiose.

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Citations

Dec 11, 2008·Applied Biochemistry and Biotechnology·Song-hua YeJin-ku Bao
Apr 20, 2001·The International Journal of Biochemistry & Cell Biology·T B Ng, Y L Yu
Dec 27, 2011·Glycobiology·Tomohiro SuzukiHirokazu Kawagishi
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Jul 27, 2010·Phytomedicine : International Journal of Phytotherapy and Phytopharmacology·Zi-ting ZhangJin-ku Bao
Sep 30, 2000·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·L S OoiV E Ooi
Apr 27, 2002·Physiologia Plantarum·Rocío EstebanEmilia Labrador

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