caa a22 4500 397558546 CHVBK 20180308164810.0 cr unu---uuuuu 161202e199611 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021504 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021504 Isolation and Identification of Myosin I from Porcine Aorta Media Smooth Muscle [Elektronische Daten] [Yasushi Hasegawa, Tomoaki Kikuta, Yoh Okamoto] A complex of 110-kDa heavy chain and calmodulin was isolated from porcine aorta media smooth muscle and identified as myosin I. The isolated myosin I consisted of equimolar amounts of 110-kDa heavy chain and calmodulin. The addition of exogenous calmodulin to the complex revealed that a maximum of two molecules of calmodulin could be bound to the heavy chain. Isolated complex bound to F-actin in an ATP-dependent manner and its Mg2+-ATPase activity was activated by F-actin. In addition, it bound to phospholipid, which is a characteristic property of myosin I. Calcium ions induced a structural change, which was revealed by a difference in the cleavage pattern and for rate of cleavage bya-chymotrypsin. This behavior was similar to that reported for brush border myosin I [L.M. Collins and A. Bretscher (1988) J. Cell. Biol. 106, 367-373]. Calcium-dependent structural change of a complex of 110-kDa heavy chain and calmodulin was found from its solubility change at various NaCl concentrations in the presence of ATP. A complex of 116-kDa heavy chain and calmodulin, possibly another type of myosin I, was also isolated. A polyclonal antibody against the complex of 110-kDa heavy chain and calmodulin did not recognize the 116-kDa heavy chain. This result suggests that at least two types of myosin Is may exist at the protein level in porcine aorta media smooth muscle. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence aorta smooth muscle nationallicence calmodulin nationallicence isoform nationallicence myosin I nationallicence Hasegawa Yasushi Department of Applied Chemistry, Muroran Institute of Technology, 27-1 Mizumoto, Muroran, Hokkaido 050 aut Kikuta Tomoaki Department of Applied Chemistry, Muroran Institute of Technology, 27-1 Mizumoto, Muroran, Hokkaido 050 aut Okamoto Yoh Department of Applied Chemistry, Muroran Institute of Technology, 27-1 Mizumoto, Muroran, Hokkaido 050 aut The Journal of Biochemistry Oxford University Press 120/5(1996-11), 901-907 0021-924X 120:5<901 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021504 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021504 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hasegawa Yasushi Department of Applied Chemistry, Muroran Institute of Technology, 27-1 Mizumoto, Muroran, Hokkaido 050 aut NATIONALLICENCE 700 1- Kikuta Tomoaki Department of Applied Chemistry, Muroran Institute of Technology, 27-1 Mizumoto, Muroran, Hokkaido 050 aut NATIONALLICENCE 700 1- Okamoto Yoh Department of Applied Chemistry, Muroran Institute of Technology, 27-1 Mizumoto, Muroran, Hokkaido 050 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/5(1996-11), 901-907 0021-924X 120:5<901 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford