TY - JOUR
T1 - The effect of crosslinking of thin filament with glutaraldehyde on the contractility of muscle fiber
AU - Prochniewicz-Nakayama, Ewa
AU - Yanagida, Toshio
PY - 1982/10
Y1 - 1982/10
N2 - The effect of crosslinking of F-actin with glutaraldehyde on the contractility of muscle ghost fiber containing reconstituted thin filament (i.e. F-actin-tropomyosin-troponin complex) and irrigated with myosin was investigated. The results show that: (i) crosslinking inhibited development of isometric tension and shortening of the fiber in the presence of MgATP, (ii) superprecipitation of the complex of myosin with crosslinked thin filament was considerably delayed, (iii) crosslinking inhibited neither binding of myosin heads to the filament nor activation of myosin ATPase. It is suggested that alterations of actin structure due to the formation of intra- and/or intermonomer crosslinks can essentially affect the process of contractility.
AB - The effect of crosslinking of F-actin with glutaraldehyde on the contractility of muscle ghost fiber containing reconstituted thin filament (i.e. F-actin-tropomyosin-troponin complex) and irrigated with myosin was investigated. The results show that: (i) crosslinking inhibited development of isometric tension and shortening of the fiber in the presence of MgATP, (ii) superprecipitation of the complex of myosin with crosslinked thin filament was considerably delayed, (iii) crosslinking inhibited neither binding of myosin heads to the filament nor activation of myosin ATPase. It is suggested that alterations of actin structure due to the formation of intra- and/or intermonomer crosslinks can essentially affect the process of contractility.
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U2 - 10.1093/oxfordjournals.jbchem.a134045
DO - 10.1093/oxfordjournals.jbchem.a134045
M3 - Article
C2 - 6217200
AN - SCOPUS:0020195637
SN - 0021-924X
VL - 92
SP - 1269
EP - 1277
JO - Journal of Biochemistry
JF - Journal of Biochemistry
IS - 4
ER -