Abstract
The striated remotor muscle of the lobster antenna has an extraordinarily profuse sarcoplasmic reticulum as shown by electron microscopy. Gel electrophoresis reveals a simple protein composition in which the Ca 2+-ATPase predominates. Vesicles of sarcoplasmic reticulum (SR) from this remoter are shown to operate Ca 2+ binding, Ca 2+ transport, and Ca 2+-activated hydrolysis of ATP with an usual efficiency (2 Ca 2+ transported per ATP hydrolysed, 4 μmol ATP hydrolysed/mg protein/min). Skinned fiber experiments were performed. They indicate behaviour of the remotor expected from observations by EM and gel electrophoresis: contraction of low maximal intensity under Ca 2+ excitation, long internal diffusion time due to the large volume of SR to be crossed, and large Ca 2+ Content released in a caffeine-sensitive manner.
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