Abstract
Isoelectric focusing of purified Na,K-ATPase on polyacrylamide gels resolved the protein into ten bands. The catalytic and glycoprotein subunits were separated by sodium dodecyl sulfate gel filtration. Isoelectric focusing of the isolated glycoprotein subunit showed that it accounted for nine of the ten bands. Part of this microheterogeneity can be attributed to variations in sialic acid content in individual bands, since removal of all of the sialic acid by neuraminidase treatment reduced the number of bands to four. It is suggested that the microheterogeneity of the glycoprotein subunit is due to post-translational modifications of oligosaccharides on a common polypeptide backbone.
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