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Extra resources for Biomembranes Part M
E. Thompson, Biochim. Biophys. Acta 382, 276 (1975). 2 p. Rosevear, T. VanAken, J. Baxter, and S. Ferguson-Miller, Biochemistry 19, 4108 (1980). METHODS IN ENZYMOLOGY, VOL. 125 Copyright © 1986 by Academic Press, Inc. All rights of reproduction in any form reserved. 28 GENERALAPPROACHES  fective. 2-4 Other investigators have found it to be the detergent of choice for studying rhodopsin 5 and photosynthetic reaction centers, 6 suggesting that this detergent may have generally useful properties for studies on a variety of intrinsic membrane proteins.
The authors wish to thank Dr. Leena Mela (Oregon Health Sciences University) and Dr. Richard Bukoski (Michigan State University) for valuable discussions during the early stages of this work; Dr. Loran L. Bieber (Michigan State University), Dr. Richard W. yon Korff (Michigan Molecular Institute, Midland, MI), and Dr. John E. Wilson (Michigan State University) for helpful advice; Mr. Randy Shoemaker for his assistance in animal care; Mrs. Helen J. Farr for her careful typing of the manuscript; and the Department of Animal Sciences, Michigan State University, particularly Mr.
VanAken and S. Ferguson-Miller, unpublished) support the idea that the maltose head groups are indeed relatively immobilized, compared to glucose in an octyl glucoside micelle. More recently, laurylmaltoside has been reported to increase the stability of photosynthetic reaction centers that were purified in lauryldimethylamine oxide (LDAO) from Rhodopseudomonas sphaeroides. 6 Similarly, a final sucrose-gradient purification step in laurylmaltoside of photosystem II from thermophilic blue-green algae results in a significant increase in purity, activity, and stability of the complex.