ISSN:
0886-1544
Keywords:
Hela spectrin
;
membrane
;
cytoskeleton
;
filamin
;
actin
;
Life and Medical Sciences
;
Cell & Developmental Biology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Medicine
Notes:
From 30-40 g of Hela-S3 cells grown in suspension, 0.25-0.50 mg of spectrin has been purified by conventional biochemical procedures starting from a low ionic strength extraction at alkaline pH of crude Hela membranes. Hela spectrin consists in its native form of a tetramer α2β2 of two high molecular weight polypeptides (240,000 and 230,000 daltons). Three different populations of Hela membranes depleted of both spectrin and actin have been prepared on discontinuous sucrose gradients. Surprisingly, spectrin will reassociate with only the heavier membrane fraction. This reassociation is specific for Hela spectrin, since three other purified Hela proteins as well as human erythrocyte spectrin do not reassociate under the same conditions. This binding is not due to the presence of traces of actin still present in the membrane fraction since two Hela actin-binding proteins (filamin I and II) do not show any significant binding to this fraction. The nature of the membrane-binding site for Hela spectrin is discussed.
Additional Material:
7 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/cm.970030530
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