Occlusion of Rb+ after extensive tryptic digestion of shark rectal gland Na,K-ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference13 articles.
1. Extensive digestion of Na+,K(+)-ATPase by specific and nonspecific proteases with preservation of cation occlusion sites.
2. Amino-acid sequence of the catalytic subunit of the (Na+ + K+)ATPase deduced from a complementary DNA
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1. Site-Directed Mutagenesis of Cation Coordinating Residues in the Gastric H,K-ATPase;Archives of Biochemistry and Biophysics;2001-03
2. Selectivity of lipid–protein interactions with trypsinized Na,K-ATPase studied by spin-label EPR;Biochimica et Biophysica Acta (BBA) - Biomembranes;1998-05
3. Structural organization, ion transport, and energy transduction of P-type ATPases;Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes;1996-05
4. The sodium PUMP;ATPases;1996
5. Do Transmembrane Segments in Proteolyzed Sarcoplasmic Reticulum Ca2+-ATPase Retain Their Functional Ca2+ Binding Properties after Removal of Cytoplasmic Fragments by Proteinase K?;Journal of Biological Chemistry;1995-08
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