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| Year : 1997 | Volume
: 45
| Issue : 3 | Page : 150--154 |
Characterisation of agglutination properties of myelin basic protein.
S Basu, G Gupta, RG Mahajan
Department of Fundamental Biochemistry, n Institute of Chemical Biology, Calcutta - 700 032, India
Correspondence Address:
S Basu
Department of Fundamental Biochemistry, n Institute of Chemical Biology, Calcutta - 700 032
India
 Source of Support: None, Conflict of Interest: None  | Check |
PMID: 29512538 
Myelin basic protein (MBP) from one month old rat brain was purified by CM-52 cellulose chromatography and heparin sepharose chromatography. It's lectin properties were studied and conditions for optimum agglutination were observed. MBP behaved likea heparin binding lectin. Carbohydrade binding specificity studies showed that on molar basis MBP was feebly inhibited by lactose and strongly inhibited by heparin. Inhibition due to heparin was not due to electrostatic forces as evidenced by no inhibition due to other glycosaminoglycans. Argine and lysine residues were involved in the agglutination activity of MBP.
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