The ATPase kinetics of insect fibrillar flight muscle myosin subfragment-1

1986 ◽  
Vol 7 (2) ◽  
pp. 179-192 ◽  
Author(s):  
D. C. S. White ◽  
R. W. Zimmermann ◽  
D. R. Trentham
1992 ◽  
Vol 23 (3) ◽  
pp. 213-221 ◽  
Author(s):  
Jean S. Drew ◽  
Marianne P. White ◽  
Carl Moos ◽  
Leonard A. Stein

1995 ◽  
Vol 270 (13) ◽  
pp. 7125-7133 ◽  
Author(s):  
Laurent Blanchoin ◽  
Stéphane Fievez ◽  
Franck Travers ◽  
Marie-France Carlier ◽  
Dominique Pantaloni

2002 ◽  
Vol 402 (2) ◽  
pp. 243-248 ◽  
Author(s):  
Bruce D Ray ◽  
Mikhail I Khoroshev ◽  
Kathleen Ue ◽  
Manuel F Morales ◽  
B.D Nageswara Rao

1985 ◽  
Vol 47 (2) ◽  
pp. 151-169 ◽  
Author(s):  
R.S. Goody ◽  
M.C. Reedy ◽  
W. Hofmann ◽  
K.C. Holmes ◽  
M.K. Reedy

1997 ◽  
Vol 321 (2) ◽  
pp. 519-523 ◽  
Author(s):  
Pawel T. SZYMANSKI ◽  
Zenon GRABAREK ◽  
Terence TAO

Calponin is a thin-filament-associated protein that has been implicated in the regulation of smooth-muscle contractility. It binds to F-actin and inhibits the MgATPase activity of actomyosin. In the present work we have examined the effect of recombinant chicken gizzard α-calponin (RαCaP) on the binding of rabbit skeletal-muscle myosin subfragment 1 (S1) to F-actin and on the inhibition of its actin-activated MgATPase. We have found that binding of one RαCaP molecule to every three to four actin monomers is sufficient for maximal inhibition of actoŐS1 ATPase. At this RαCaP/actin ratio RαCaP does not interfere with S1 binding to F-actin. At higher concentrations, RαCaP displaces S1 from F-actin and a 1:1 RαCaPŐactin monomer complex is formed. RαCaP is also able to displace troponin I from its complex with F-actin which may reflect the amino acid sequence similarity between RαCaP and troponin I in their actin-binding regions.


Sign in / Sign up

Export Citation Format

Share Document