Myosin of fast and slow muscles of the rabbit

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Abstract

Myosin of slow muscles of the rabbit has two or three times lower actin-activated and EDTA-activated ATPase and Ca++-activated ATPase and ITPase activities than those of rabbit fast muscles. Unlike myosin of fast muscles, the Ca++- and EDTA-activated ATPase activities of myosin of slow muscles are not increased in the alkaline pH range.

Despite these qualitative differences, both kinds of muscle contain the same amount of myosin. Fast muscle contains more sarcoplasmic and less stroma proteins than slow muscle, whereas actin content is the same. After 19 days of denervation the myosin isolated from fast muscle shows only a slight decrease in its NTPase activities and no change in its pH-activity curve compared with the myosin of the same normal muscle.

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    Citation Excerpt :

    Force decreases during active isokinetic shortening because of a decrease in the number of attached cross bridges and in the amount of force produced per cross bridge (Huxley, 1957). It is known that fast fibers have high rates of ATP hydrolysis and cross bridge attachment and therefore as filaments slide past one another at the same speed for fast and slow fibers, fewer cross bridges have the time to attach in slow fibers and thus force decreases more in slow compared to fast fibers (Barany et al., 1965). Force per cross bridge decreases during shortening because the distance “x” (Huxley, 1957) decreases when the filaments slide past one another.

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This work was supported by research grant A-4873 from the NIH, U. S. Public Health Service, by grants from Muscular Dystrophy Associations of America, Inc. and by a grant from the Muscular Dystrophy Association of Canada.

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