Chymotryptic cleavage of α-subunit in E1-forms of renal (Na+ + K +)-ATPase: effects on enzymatic properties, ligand binding and cation exchange
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference35 articles.
1. Purification and characterization of (Na+, K+)-ATPase. V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool
2. Purification and characterization of (Na+ + K+)-ATPase. VI. Differential tryptic modification of catalytic functions of the purified enzyme in presence of NaCl and KCl
3. Proteolytic fragmentation of the catalytic subunit of the sodium and potassium adenosine triphosphatase. Alignment of tryptic and chymotryptic fragments and location of sites labeled with ATP and iodoacetate
4. Identification of a membrane-embedded segment of the large polypeptide chain of (Na+, K+)ATPase
5. Evidence for the organization of the transmembrane segments of (Na,K)-ATPase based on labeling lipid-embedded and surface domains of the alpha-subunit.
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