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• W944878829 abstract "the discovery of (Na+ + K+)-ATPase, intensive studies have been carried out to elucidate its rote in the active transport of sodium and potassium. The enzyme has not been purified to a homogeneous state, but recently some progress in this direction has been made and information about the molecular components of the sodium pump is beginning to emerge. The difficulties encountered in isolation of (Na+ + K+)-ATPase are mainly explained by the firm association of the enzyme with cell membranes. The membranes are sheared into fragments and vesicles of varying sizes during homogenization. This explains that the (Na+ + K+)-ATPase is found in all sediments after conventional differential centrifugations and that a major fraction of the activity in the subcellular fractions is latent a owing to limited access of substrate or activators to the inside of the membrane vesicles. Furthermore, it is difficult to separate the enzyme from other proteins associated with the cell membranes." @default.
• W944878829 created "2016-06-24" @default.
• W944878829 creator A5030944837 @default.
• W944878829 date "1974-01-01" @default.
• W944878829 modified "2023-10-18" @default.
• W944878829 title "[26] Isolation of (Na+ + K+)-ATPase" @default.
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• W944878829 doi "https://doi.org/10.1016/0076-6879(74)32029-0" @default.
• W944878829 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4280486" @default.
• W944878829 hasPublicationYear "1974" @default.
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