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JBC, Vol. 250, Issue 14, 5459-5469, Jul, 1975
S. Clarke
Sucrose density gradient centrifugation has been used to measure the
binding of Triton X-100 above its critical micellar concentration to a
variety of purified membrane and non-membrane proteins. In addition,
binding studies were done on the three proteins below the critical micellar
concentration of detergent to distinguish between the interaction of
proteins with detergent monomers and detergent micelles. A procedure is
described for the calculation of the molecular weight of these Triton X-100
protein complexes and measurements were made for opsin, plasma low density
lipoprotein, the (Na-+ plus K-+)-dependent adenosine triphosphatase, the
human red blood cell major sialoglycoprotein (PAS-1) and the human red
blood cell minor glycoprotein (bandIII). These proteins behave as monomers
or dimers in detergent and bind between 0.28 and 1.12 g of detergent per g
of protein. A general method is also present for calculating the molecular
size and shape of impure membrane proteins in detergent. Finally, Triton
X-100 was shown to replace bound Na dodecyl-SO4 on the minor glycoprotein
of the red blood cell.
The size and detergent binding of membrane proteins
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