Evidence for a diprotomeric structure of Na,K‐ATPase

FEBS Letters

Chetverin, Alexander B.¹ 

[1] Institute of Protein Research, Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR

关键词: (Na+ + K+)-ATPase;    Enzyme structure;    Subunit modification;    Protein assay;    End-group analysis;   

DOI  :  10.1016/0014-5793(86)80225-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three methods were used to assess protein concentration in membrane-bound Na,K-ATPase preparations: standard Lowry assay, Kjeldahl nitrogen determination and amino acid analysis. While the first two methods showed excellent agreement, the third one always gave a lower value which varied drastically depending on the condition of sample treatment before amino acid analysis. This result reinforces the Lowry method in assessing the true concentration of Na,K-ATPase protein and suggests 250 kDa to be a true estimate of the molecular mass of the smallest ligand-binding unit of the enzyme. The cyanate method reveals two NH₂-terminal residues of the β-subunit (NH₂-Ala) and one such residue of the α-subunit (NH₂-Gly) per ligand-binding unit. From the data on equimolarity of the α- and β-subunits in Na,K-ATPase this suggests that the enzyme molecule is composed of two αβ-protomers, one possessing a modified (presumably an N-blocked) α-subunit.

【 授权许可】

Unknown