title: Shortening velocity and force/pCa relationship in skinned crab muscle fibres of different types.
abstract: Single fibres of three different types, which had been characterized histochemically with regard to differences in myofibrillar adenosine triphosphatase (ATPase) activity and its pH stability, were microdissected from freeze dried preparations of the closer muscle in walking legs of the crab Eriphia spinifrons. Shortening velocities were determined in slack tests and under constant load conditions in maximally Ca(2+)-activated skinned muscle fibres. Force/pCa relationships were also measured for the different types of fibres. Compared with data on vertebrate muscles, all crab muscle fibres required large length changes to reach zero force and showed low Ca2+ sensitivity for isometric force generation. The length/time relationship obtained from slack tests had a biphasic course. Maximal velocity of filament sliding differed in the three types of fibres investigated. The filament sliding of type IV fibres was about 3 times faster than that of type I fibres. The values obtained for type II fibres ranged in between. These data are positively correlated with myofibrillar ATPase activity determined histochemically. Ca2+ sensitivity of force generation was lowest in the fast type IV fibres. It was high in the slow type I and the faster contracting type II fibres. Ca2+ sensitivity in crab muscle seems not to be correlated with speed of shortening.
authors.affiliation: Faculty of Biology, University of Konstanz, Federal Republic of Germany.
authors.forename: S
authors.initials: S
authors.lastname: Galler
authors.forename: W
authors.initials: W
authors.lastname: Rathmayer
mesh_terms: D000251:Adenosine Triphosphatases / Q000502:physiology; D000818:Animals; D003386:Brachyura; D002118:Calcium / Q000502:physiology*; D009119:Muscle Contraction; D009132:Muscles / Q000201:enzymology / Q000502:physiology*
chemical_list: D000251:Adenosine Triphosphatases; D002118:Calcium