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Primary structure of the beta-subunit of Na+,K+-ATPase from the swine kidney. I. Analysis of products of trypsin hydrolysis of immobilized proteins

Arzamazova, N.M.; Gevondian, N.M.; Chertova, E.N.; Nazimov, I.V.; Gavril'eva, E.E.

Bioorganicheskaia Khimiia 13(1): 5-13

1987

ISSN/ISBN: 0132-3423
PMID: 3032209
Document Number: 298601
The Na+, K+-ATPase's beta-subunit immobilized on thiol-glass was hydrolyzed with trypsin. Over 25 peptides covering ca. 90% of the protein polypeptide chain were isolated from the digest by HPLC and characterized. Structural analysis allowed us to localize the sites of attachment of all three carbohydrate chains of beta-subunit. Sequence data were used to design of oligonucleotide hybridization probes for gene cloning.

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