[Primary structure of the alpha subunit of Na+,K+-ATPase. I. Analysis of hydrophilic fragments of the polypeptide chain]

Bioorg Khim. 1985 Dec;11(12):1598-606.
[Article in Russian]

Abstract

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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Hydrolysis
  • Kidney Medulla / enzymology
  • Peptide Fragments / analysis*
  • Peptides / analysis*
  • Sodium-Potassium-Exchanging ATPase / analysis*
  • Swine
  • Trypsin

Substances

  • Peptide Fragments
  • Peptides
  • Trypsin
  • Sodium-Potassium-Exchanging ATPase