[Primary structure of the beta-subunit of Na+,K+-ATPase from the swine kidney. I. Analysis of products of trypsin hydrolysis of immobilized proteins].
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.
D000595:Amino Acid Sequence; D000818:Animals; D004800:Enzymes, Immobilized / Q000032:analysis*; D006868:Hydrolysis; D007668:Kidney / Q000201:enzymology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis*; D013552:Swine; D014357:Trypsin
D004800:Enzymes, Immobilized; D014357:Trypsin; D000254:Sodium-Potassium-Exchanging ATPase
Pervichnaia struktura beta-sub''edinitsy Na+,K+-ATP-azy pochek svin'i. I. Analiz produktov tripticheskogo gidroliza immobilizovannogo belka.