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Additional info for Biomembranes Part P: ATP-Driven Pumps and Related Transport: The Na,K-Pump
For a discussion of the problem see Refs. 25, 35, and 74.  PURIFICATIONOF Na +,K+-ATPase 29  Purification of N a + , K + - A T P a s e : E n z y m e Sources, Preparative Problems, and Preparation from Mammalian Kidney B y PETER L E T H J~RGENSEN Introduction Purification of Na+,K+-ATPase to homogeneity requires starting material from tissues with exceptionally large capacities for active Na ÷ transport like the outer renal medulla in mammalian kidney, 1-4 rectal glands of dogfish,5,6 eel electroplax,7,8 and salt glands of ducks in which Na+,K+-ATPase can be induced by salt treatment.
53 Sedimentation velocity analysis of mammalian kidney enzyme dissolved in C12E8 gives a molecular weight of 170,00061 and low-angle neutron scattering analysis of mammalian kidney enzyme dissolved in Brij gives a molecular weight of 310,000. 62 Radiation inactivation measurements on partly purified membrane preparations give a molecular weight for Na ÷,K+-ATPase from red blood cells of 300,00063 and 330,000, 64 from mammalian kidney of 190,00063 and 261,000, 65 and from mammalian brain of 264,000.
Transp. 19, 119 (1983). zz B. Forbush, J. Biol. Chem. 257, 12678 (1982). 23 B. Forbush, Anal. Biochem. 140, 495 (1984). 24 S. Seiler and S. Fleischer, J. Biol. Chem. 259, 8550 (1984). 25 K. D. Dzhandzhugazyan and P. L. JCrgensen, Biochim. Biophys. Acta 017, 165 (1985). z6 p. L. JCrgensen, this series, Vol. 36, p. 434. 27 j. B. Brotherus, P. C. Jost, O. H. Griflith, and L. E. Hokin, Biochemistry 18, 5043 (1979).  PURIFICATION OF N a + , K + - A T P a s e 31 late is an ideal detergent. Its cmc is relatively high and the optimum concentration for demasking is to a large extent independent of protein concentration.