Analysis of the ternary interaction of the red cell membrane skeletal proteins spectrin, actin, and 4.1.

Abstract:

:Spectrin dimers interact weakly with F-actin under physiological solvent conditions (with an association constant of about 5 X 10(3) M-1 at 20 degrees C). In the presence of the membrane skeletal constituent, protein 4.1, strong binding is observed; an analysis of the profiles for formation of a ternary complex leads to an association constant of about 1 X 10(12) M-2. This association becomes weaker at low ionic strength, whereas the opposite applies to the spectrin-actin interaction. The stability of the ternary complex is maximal at physiological ionic strength and somewhat above. The effect of temperature in the range 0-20 degrees C on the formation of the ternary complex is small, whereas the spectrin-actin interaction almost vanishes at low temperature. There is no detectable calcium sensitivity in either the binary or the ternary system within the limits of precision of our assay. The ternary complex resembles the natural system in the membrane in that the actin is resistant to dissociation and unavailable in the deoxyribonuclease assay; after selective proteolytic destruction of spectrin and 4.1, all the actin becomes available. In the absence of 4.1, spectrin dimers do not measurably protect the actin against dissociation.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Ohanian V,Wolfe LC,John KM,Pinder JC,Lux SE,Gratzer WB

doi

10.1021/bi00314a027

subject

Has Abstract

pub_date

1984-09-11 00:00:00

pages

4416-20

issue

19

eissn

0006-2960

issn

1520-4995

journal_volume

23

pub_type

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