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Author Kannan, V. M. ♦ Appukuttan, P. S.
Source Sree Chitra Tirunal Institute for Medical Sciences & Technology
Content type Text
Publisher Indian Journal of Biochemistry & Biophysics
File Format PDF
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Technology ♦ Medicine & health
Subject Domain (in MeSH) Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Chemical Phenomena ♦ Biological Sciences
Subject Keyword Biochemistry
Abstract In order to identify the complementary glycoproteins (receptors) that are recognized in bovine brain stem by endogenous 14 kDa galactose-binding lectin (BBL), probable glycoproteins were first selected by affinity chromatography of soluble tissue glycoproteins on Rinicus communis agglutinin (RCB) - Sepharose since this lectin had similar sugar specificity to the endogenous,lectin. From Western blot of RCA-binding glycoproteins, the lectin, as its peroxidase conjugate sugar-specifically recognized chiefly an 84 kDa glycoprotein subunit and a few minor subunits. On alkaline pH PAGE of the RCA-binding brain stem glycoproteins, a prominent fast moving protein was separated which, on electroelution and dot blotting, was also recognized by BBL sugar-specifically. This glycoprotein was composed of 55 kDa and 58 kDa subunits as seen by SDS-PAGE and was also immunologically distinct from the 84 kDa subunit. Qualitative test on dot blots of the electroeluted glycoproteins using peroxidase conjugates of plant lectins of varying specificities as well as the human serum anti-alpha-galactoside antibody indicated differences in carbohydrate composition between the 84 kDa subunit and the alkaline; PAGE fast moving glycoprotein. Membrane-bound brain stem glycoproteins were not recognized by BBL.
Education Level UG and PG
Learning Resource Type Article
Educational Framework Medical Council of India (MCI)
Volume Number 31
Issue Number 3
Page Count 5
Starting Page 160
Ending Page 164