Improved separation at low temperature of glycoproteins by Con A-Sepharose affinity chromatography in the presence of sodium dodecyl sulfate (SDS) |
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Authors: | S. Aono R. Semba S. Kishiwamata |
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Affiliation: | (1) Department of Perinatology, Institutte for Developmental Research, Aichi Prefecture Colony, 480-03 Kasugai, Aichi, (Japan) |
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Abstract: | Summary The Con A-Sepharose affinity chromatography of glycoproteins was even more effective at 4°C than that at room temperature (26–28°C) in the presence of sodium dodecyl sulfate (SDS). Application of this methodology to the seperation of several glycoproteins from SDS-solubilized membrane proteins in rat cerebellum, including a glycoprotein characteristics of the Purkinje cells, was sucessful.Acknowledgments. A part of this research was supported by a Grantin-Aid for Scientific Research from the Ministry of Education, Science and Culture (No. 58480150), and also by a grant from National Center of Nervous, Mental and Muscular Disorders (NCNMMD) of the Ministry of Health and Welfare (No.83-11) in Japan. |
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Keywords: | Con A-Spharose SDS-glucoproteins cerebellar proteins affinity chromatography purification |
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