[Primary structure of the alpha subunit of Na+,K+-ATPase. I. Analysis of hydrophilic fragments of the polypeptide chain].
The selective tryptic digestion of the native membrane-bound enzyme was carried out under conditions that provide the extensive hydrolysis of hydrophilic regions of the alpha-subunit into small fragments and allow to preserve the integrity of the beta-subunit. Twenty-seven water-soluble peptides comprising approximately 40% of the total polypeptide chain were isolated by HPLC and their complete or partial amino acid sequence was determined. It led to general outline of the structural organisation of the alpha-subunit hydrophilic regions exposed from membrane. The information thus obtained was used in synthesis of specific oligonucleotide probes.
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007679:Kidney Medulla / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis*; D010455:Peptides / Q000032:analysis*; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis*; D013552:Swine; D014357:Trypsin
D010446:Peptide Fragments; D010455:Peptides; D014357:Trypsin; D000254:Sodium-Potassium-Exchanging ATPase
Pervichnaia struktura alpha-sub''edinitsy Na+,K+-ATP-azy. I. Analiz gidrofil'nykh fragmentov polipeptidnoĭ tsepi.