Resolution of microheterogeneity in rat liver acid phosphatase using immobilised sialic acid binding lectin
Mohan, S.; Bishayee, S.; Bachhawat, B.K.
Indian Journal of Biochemistry and Biophysics 18(3): 177-181
1981
ISSN/ISBN: 0301-1208 PMID: 7309092 Document Number: 176304
The sialic acid binding lectin, carcinoscorpin (CSN), immobilized to sepharose, has been used to resolve the free form of rat liver acid phosphatase into 3 different forms based on their varied sialic acid content. The disaccharide from sheep submaxillary mucin, O-(N-acetylneuraminyl)-(2 .fwdarw. 6)-2-acetamido-2-deoxygalactitol, which is an inhibitor of the binding of sialoglycoproteins to CSN, was used for the gradient elution of the enzymes bound to CSN-sepharose. The 3 forms of the enzyme fractionated by different concentrations of the disaccharide differed in sialic acid content. A polyacrylamide gel electrophoretic pattern, based on the change heterogeneity, was in accordance with these results showing microheterogeneity in rat liver acid phosphatase due to sialic acid.