Interaction of myosin subfragments with F-actin.

Abstract:

:The effect of ionic strength, temperature, and divalent cations on the association of myosin with actin was determined in the ultracentrifuge using scanning absorption optics. The association constant (Ka) for the binding of heavy meromyosin (HmM) to F-actin was 1 X 10(7) M-1 at 20 degrees C, in 0.10 M KCl, 0.01 M imidazole (pH 7.0), 5 MM potassium phosphate, 1 mM MgCl2, and 0.3 mM ethylene glycol bis(beta-aminoethyl ether)-N,N'-tetraacetic acid. Ka was the same for HMM prepared by trypsin or chymotrypsin. The affinity of subfragment 1 (S1) for actin under the same ionic conditions was 3 X 10(6) M-1. Varying the preparative procedure for S1 had little effect on Ka. The small difference in binding energy between HMM and S1 suggests that either only one head can bind strongly to actin at a time or that free energy is lost during the sterically unfavorable attachment of the two heads to actin.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Margossian SS,Lowey S

doi

10.1021/bi00618a017

subject

Has Abstract

pub_date

1978-12-12 00:00:00

pages

5431-9

issue

25

eissn

0006-2960

issn

1520-4995

journal_volume

17

pub_type

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