Properties of calponin isolated from sheep aorta thin filaments
- 4 November 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 292 (1-2) , 179-182
- https://doi.org/10.1016/0014-5793(91)80862-w
Abstract
Calponin, a 35 kDa actin‐binding protein, was shown to be a normal component of ‘native’ thin filaments prepared from sheep aorta. Actin, tropomyosin, caldesmon and calponin were present in molar ratios 14 : 2 : 1 : 0.9. Calponin was isolated from thin filaments in yield 0.5 mg/100 mg thin filament protein. Calponin inhibited actomyosin ATPase up to 85%, half maximal at 0.2 calponin/actin. Inhibition did not depend on tropomyosin, Ca2+ or Ca2+·calmodulin. Caldesmon inhibited actomyosin with a 10‐fold greater potency than calponin in the presence of tropomyosin and inhibition could be reversed by Ca2+·calmodulin under certain conditions. Calponin had no effect on caldesmon inhibition or the reversal of inhibition.Keywords
This publication has 26 references indexed in Scilit:
- Calponin and the composition of smooth muscle thin filamentsJournal of Muscle Research and Cell Motility, 1991
- The mechanism for the inhibition of actin-activated ATPase of smooth muscle heavy meromyosin by calponinBiochemical and Biophysical Research Communications, 1991
- Smooth muscle specific expression of calponinFEBS Letters, 1990
- Do thin filaments of smooth muscle contain calponin?FEBS Letters, 1990
- 35 kDa proteins are not components of vertebrate smooth muscle thin filamentsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- Summer festivals in the GDRReligion in Communist Lands, 1988
- Reversal of caldesmon function by anti-caldesmon antibodies confirms its role in the calcium regulation of vascular smooth muscle thin filamentsBiochemical and Biophysical Research Communications, 1988
- Vascular smooth muscle calponin. A novel troponin T-like protein.Hypertension, 1988
- Isolation and characterization of a 34000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscleBiochemical and Biophysical Research Communications, 1986
- Disassembly and reconstitution of the Ca2+‐sensitive thin filaments of vascular smooth muscleFEBS Letters, 1985