Búsqueda | Portal Regional de la BVS

[Primary structure of the beta-subunit of Na+,K+-ATPase from the swine kidney. I. Analysis of products of trypsin hydrolysis of immobilized proteins]. / Pervichnaia struktura beta-sub''edinitsy Na+,K+-ATP-azy pochek svin'i. I. Analiz produktov tripticheskogo gidroliza immobilizovannogo belka.

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

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

Artículo en Ruso | MEDLINE | ID: mdl-3032209

RESUMEN

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.

Asunto(s)

Enzimas Inmovilizadas/análisis , Riñón/enzimología , ATPasa Intercambiadora de Sodio-Potasio/análisis , Secuencia de Aminoácidos , Animales , Hidrólisis , Porcinos , Tripsina

RESUMEN

Asunto(s)

ENVIAR RESULTADO:

SELECCIÓN DE REFERENCIAS

DETALLE DE LA BÚSQUEDA