CH CHC一CH CH: CH2 CH: HCN Figure 10-20. The structures of two commonly used CH detergents Sodium dodecyl CH CH2 CH CH sulfate(SDS )is an anionic detergent, and Triton X-100 is CH2 a nonionic detergent. The CHa hydrophobic portion of each CH2 detergent Is shown in green 8 CHa CH and the d le hydrophilic portion CHZ shown in blue. note that the O=s=0 bracketed portion of Triton X 100 is repeated about eight sodium dodecyl sulfate Triton X-100 (SDS) times
Figure 10-20. The structures of two commonly used detergents. Sodium dodecyl sulfate (SDS) is an anionic detergent, and Triton X-100 is a nonionic detergent. The hydrophobic portion of each detergent is shown in green, and the hydrophilic portion is shown in blue. Note that the bracketed portion of Triton X- 100 is repeated about eight times
Figure 10-21. The use of U44 mild detergents for CYTOSOL solubilizing, purifying, and reconstituting functional detergent micelles membrane protein systems In this example functional Na*-K ATPase molecules PURSFICATION OF Na'.K ATPase are purified and incorporated into phospholipid vesicles The Na*-K+ ATPase is an ion pump that is present in the REMOVAL O DETERGENT plasma membrane of most ADDITION o PHOSPHOLIPIDS animal cells. it uses the (mixed with detergent energy of aTP hydrolysis to monomers pump Nat out of the cell and aNaK· ATPase K in, as discussed in orated into Chapter 11
Figure 10-21. The use of mild detergents for solubilizing, purifying, and reconstituting functional membrane protein systems. In this example functional Na+ -K+ ATPase molecules are purified and incorporated into phospholipid vesicles. The Na+ -K+ ATPase is an ion pump that is present in the plasma membrane of most animal cells; it uses the energy of ATP hydrolysis to pump Na+ out of the cell and K+ in, as discussed in Chapter 11
m Figure 10-22. A scanning electron micrograph of human red blood cells. The cells have a biconcave shape and lack nuclei. Courtesy of Bernadette Chailley
Figure 10-22. A scanning electron micrograph of human red blood cells. The cells have a biconcave shape and lack nuclei. (Courtesy of Bernadette Chailley.)
proximate molecular weight <t spectrin 240.000 Figure 10-24 SDs polyacrylamide 220.000 B spectrin 210.000 ankyrin gel electrophoresis pattern of the proteins in the human red blood cell membrane. The gel in(a)is stained with Coomassie blue The 100000 band 3 30.000 glycophorin positions of some of the major 82000 band 4.1 proteins in the gel are indicated in the drawing in(B); glycophorin is shown in red to distinguish it from band 3 43000·ctin Other bands in the gel are omitted from the drawing. The large amount of carbohydrate in glycophorin molecules slows their migration so that they run almost as slowly as the much larger band 3 moleculeS. (A courtesy of Ted Steck.) A
Figure 10-24. SDS polyacrylamidegel electrophoresis pattern of the proteins in the human red blood cell membrane. The gel in (A) is stained with Coomassie blue. The positions of some of the major proteins in the gel are indicated in the drawing in (B); glycophorin is shown in red to distinguish it from band 3. Other bands in the gel are omitted from the drawing. The large amount of carbohydrate in glycophorin molecules slows their migration so that they run almost as slowly as the much larger band 3 molecules. (A, courtesy of Ted Steck.)
(x CHAIN H2N HOOC flexible link between domains 106-amino-acid-long 阝cHA|N domain (AI 00 Figure 10-25 Spectrin molecules from human red blood cells. The protein is shown schematically in(A)and in electron micrographs in (B) Each spectrin heterodimer consists of two antiparallel, loosely intertwined flexible polypeptide chains called a and b these are attached noncovalently to each other at multiple points, including both ends. The phosphorylated" head"end where two dimers associate to form a tetramer, is on the left. Both the a and b chains are composed largely of repeating domains 106 amino acids long. In (b)the spectrin molecules ave been shadowed with platinum. (D.W. Speicher and V.T. Marchesi Nature 311: 177-180; B, D M. Shotton et al., J. Mol. Biol. 131: 303-329)
Figure 10-25. Spectrin molecules from human red blood cells. The protein is shown schematically in (A) and in electron micrographs in (B). Each spectrin heterodimer consists of two antiparallel, loosely intertwined, flexible polypeptide chains called a and b these are attached noncovalently to each other at multiple points, including both ends. The phosphorylated "head" end, where two dimers associate to form a tetramer, is on the left. Both the a and b chains are composed largely of repeating domains 106 amino acids long. In (B) the spectrin molecules have been shadowed with platinum. (D.W. Speicher and V.T. Marchesi, Nature 311:177-180; B, D.M. Shotton et al., J. Mol. Biol. 131:303-329)