Analysis of the protein subunit structure of the oligomycin sensitive ATPase proteolipid fraction by reverse phase high pressure liquid chromatography
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference15 articles.
1. Resolution of the mitochondrial N,N′-dicyclohexylcarbodiimide binding proteolipid fraction into three similar sized proteins
2. Identification of the dicyclohexylcarbodiimide-binding protein in the oligomycin-sensitive adenosine triphosphatase from bovine heart mitochondria
3. The mechanism of mitochondrial swelling
4. Studies on the mitochondrial oligomycin-insensitive atpase
5. The identification of the site of action of NN′-dicyclohexylcarbodi-imide as a proteolipid in mitochondrial membranes
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1. Reverse-phase high-performance liquid chromatography of nerve growth factor receptor-like proteins identified with monoclonal antibodies;Journal of Neuroscience Research;1990-12
2. REVERSED-PHASE CHROMATOGRAPHY OF PROTEINS AND NUCLEIC ACIDS: PRACTICAL CONSIDERATIONS;High-Performance Liquid Chromatography;1986
3. Sequence analysis of membrane proteins;Techniques for the Analysis of Membrane Proteins;1986
4. Isolation of cardiac membrane proteolipids by high pressure liquid chromatography. A comparison of reticular and sarcolemmal proteolipids, phospholamban and calciductin;Biochimica et Biophysica Acta (BBA) - Biomembranes;1983-09
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