Download Biomembrane Protocols. Architecture and Function by Graham J.M., Higgins J.A. PDF

By Graham J.M., Higgins J.A.

This moment quantity of protocols deals the main finished set of recent analytical suggestions to be had for learning the structure and serve as of membranes. It gains the appliance of biochemical, spectroscopic, and fluorimetric the right way to the research of molecular topology, the dynamic facets of membrane constitution, and ion delivery. Antibody know-how, research of molecules interested in intracellular signaling, and receptor-ligand interactions also are coated.

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Maher, P. A. and Singer, S J. (1985) Anomalous interaction of the acetyl choline receptor protein with the nonionic detergent Triton X-114 Proc. Nut1 Acad. Sci. USA 82,958-962 5. Volk, T. and Geiger, B. (1986) A-CAM: A 135kD receptor of intercellular adherens junctions. I. Immunoelectron macroscopic localization and biochemical studies. J. Cell Biol. 103, 1441-1450. 6. Muller, W. A and Gimbrone, M. , Jr. (1986) Plasmalemmal proteins of cultured vascular endothelial cells exhibit apical-basal polarity.

5. 5M). This solution can be stored for l-2 mo at -2OOC. 6. m-Maleimtdobenzoyl-Whydroxysulfosuccinimide ester (Sulfo-MBS) solution (20 mg/mL, aqueous). This solution should be freshly prepared. Sulfo-MBS can be purchased from Pierce (Rockford, IL). 7. Keyhole limpet hemocyanin or ovalbumin (carrier proteins). 8. Sephadex G-50 and G- 10 swollen in the appropriate buffer and suitable columns. 9. Bench-top centrifuge. 10. Oxygen-free nitrogen. 11. Dialysis tubing. 2. Preparation of Antipeptide Antisera 1.

Use of fractionated IgG may prolong the life of the peptide columns and possibly reduce contamination of the final product by other serum proteins. B5. 4. Pool the peak fractions, immediately neutralize by addition of 2M Trts, and then dialyze as described. PART C. PURIFICATION BY IMMUNOAFFINITY OF MEMBRANE PROTEINS CHROMATOGRAPHY 1. Introduction Once antipeptide antibodies have been purified from an antiserum, they can be used to isolate membrane proteins by immunoaffinity chromatography. The harsh conditions required to elute bound membrane proteins from immunoaffinity columns commonly denature them, but the isolated protein is usually still amenable to analysis by SDS/polyacrylarnide gel electrophoresis, amino acid sequencing, and so on.

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