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

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

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

Bioorg Khim. 1987 Jan;13(1):5-13.

[Article in Russian]

Authors

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

PMID: 3032209

Abstract

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.

MeSH terms

Amino Acid Sequence
Animals
Enzymes, Immobilized / analysis*
Hydrolysis
Kidney / enzymology*
Sodium-Potassium-Exchanging ATPase / analysis*
Swine
Trypsin

Substances

Enzymes, Immobilized
Trypsin
Sodium-Potassium-Exchanging ATPase