Asymmetric orientation of amino groups in the α-subunit and the β-subunit of (Na+ + K+)-ATPase in tight right-side-out vesicles of basolateral membranes from outer medulla
- 1 July 1985
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 817 (1), 165-173
- https://doi.org/10.1016/0005-2736(85)90079-3
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Lactoperoxidase-catalyzed iodination of sodium and potassium ion-activated adenosine triphosphatase in the Madin-Darby canine kidney epithelial cell line and canine renal membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1983
- Infrastructure of Na,K-ATPase in Plasma Membranes VesiclesPublished by Elsevier ,1983
- STRUCTURE OF THE Na, K PUMP: CRYSTALLIZATION OF PURE MEMBRANE‐BOUND Na, K‐ATPase AND IDENTIFICATION OF FUNCTIONAL DOMAINS OF THE α‐SUBUNITAnnals of the New York Academy of Sciences, 1982
- High-affinity 86Rb-binding and structural changes in the α-subunit of Na+,K+ -atpase as detected by tryptic digestion and fluorescence analysisBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Sodium and potassium ion pump in kidney tubules.Physiological Reviews, 1980
- [13] Radioiodination by use of the Bolton-Hunter and related reagentsMethods in Enzymology, 1980
- Purification and characterization of
Na K ATPase III. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecylsulphateBiochimica et Biophysica Acta (BBA) - Biomembranes, 1974 - The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassayBiochemical Journal, 1973
- Purification and characterization of
(Na . I. The influence of detergents on the activity of(Na in preparations from the outer medulla of rabbit kidneyBiochimica et Biophysica Acta (BBA) - Biomembranes, 1971 - Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970