The effect of crosslinking of thin filament with glutaraldehyde on the contractility of muscle fiber.

Abstract:

: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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Próchniewicz-Nakayama E,Yanagida T

doi

10.1093/oxfordjournals.jbchem.a134045

subject

Has Abstract

pub_date

1982-10-01 00:00:00

pages

1269-77

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

92

pub_type

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