Lectin from rice

Indravathamma, P. and Seshadri, H. S. (1980) Lectin from rice. Journal of Biosciences, 2 (1). pp. 29-36. ISSN 0250-5991

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N-Acetyl-D-glucosamine-binding lectin was isolated and purified from rice by ammonium sulphate fractionation and affinity chromatography using N-acetyl-D-glucosamine linked Sepharose 6B column. It gave a single hand on Polyacrylamide disc gel. It was identified as a glycoprotein. The purified lectin dissociated into two components on Sephadex G-100 column chromatography,-a higher molecular weight fraction not containing any carbohydrate and a lower molecular weight glycoprotein fraction. The apparent molecular weights of these fractions were 85,000 and 14,500. The lectin agglutinated erythrocytes of human A,B,O groups and of several other mammals and its activity was inhibited only by N-acetyl-D-glucosamine. The glycopeptide isolated by pronase digestion of the lectin was homogeneous and did not possess agglutinating activity. It contained about 10% carbohydrate of which xylose, arabinose and glucose were the major components.

Item Type: Article
Additional Information: Publisher: Springer India
Subjects: C Chemical Science > Biochemistry
Divisions: Department of > Biochemistry
Depositing User: Dhruva Kumar
Date Deposited: 12 May 2021 15:58
Last Modified: 12 May 2021 15:58
URI: http://eprints.uni-mysore.ac.in/id/eprint/13870

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